| 1. |
- Bowler, Matthew W., et al.
(författare)
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Automation and Experience of Controlled Crystal Dehydration: Results from the European Synchrotron HC1 Collaboration
- 2015
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Ingår i: Crystal Growth & Design. - : American Chemical Society (ACS). - 1528-7483 .- 1528-7505. ; 15:3, s. 1043-1054
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Tidskriftsartikel (refereegranskat)abstract
- Controlled dehydration of macromolecular crystals can lead to significant improvements in crystalline order, which often manifests itself in higher diffraction quality. Devices that can accurately control the humidity surrounding crystals on a beamline have led to this technique being increasingly adopted as experiments become easier and more reproducible. However, these experiments are often carried out by trial and error, and in order to facilitate and streamline them four European synchrotrons have established a collaboration around the HC1b dehydration device. The MAX IV Laboratory, Diamond Light Source, BESSY II, and the EMBL Grenoble Outstation/ESRF have pooled information gathered from user experiments, and on the use of the device, to propose a set of guidelines for these experiments. Here, we present the status and automation of the installations, advice on how best to perform experiments using the device, and an analysis of successful experiments that begins to show some trends in the type of protocols required by some systems. The dehydration methods shown are applicable to any device that allows control of the relative humidity of the air surrounding a macromolecular crystal.
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| 2. |
- Leonarski, Filip, et al.
(författare)
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Kilohertz serial crystallography with the JUNGFRAU detector at a fourth-generation synchrotron source
- 2023
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Ingår i: IUCrJ. - 2052-2525. ; 10:Pt 6, s. 729-737
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Tidskriftsartikel (refereegranskat)abstract
- Serial and time-resolved macromolecular crystallography are on the rise. However, beam time at X-ray free-electron lasers is limited and most thirdgeneration synchrotron-based macromolecular crystallography beamlines do not offer the necessary infrastructure yet. Here, a new setup is demonstrated, based on the JUNGFRAU detector and Jungfraujoch data-acquisition system, that enables collection of kilohertz serial crystallography data at fourthgeneration synchrotrons. More importantly, it is shown that this setup is capable of collecting multiple-time-point time-resolved protein dynamics at kilohertz rates, allowing the probing of microsecond to second dynamics at synchrotrons in a fraction of the time needed previously. A high-quality complete X-ray dataset was obtained within 1 min from lysozyme microcrystals, and the dynamics of the light-driven sodium-pump membrane protein KR2 with a time resolution of 1 ms could be demonstrated. To make the setup more accessible for researchers, downstream data handling and analysis will be automated to allow on-the-fly spot finding and indexing, as well as data processing.
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| 3. |
- Logan, Derek, et al.
(författare)
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Status of the crystallography beamlines at the MAX IV Laboratory
- 2015
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Ingår i: The European Physical Journal Plus. - : Springer Science and Business Media LLC. - 2190-5444. ; 130:3
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Forskningsöversikt (refereegranskat)abstract
- The MAX IV Laboratory in Lund is currently operating two storage rings, the 1.5 GeV MAX II and the 700MeV MAX III, as well as constructing the new facility MAX IV, which will house a 1.5 GeV and a 3 GeV ring. At the MAX II synchrotron there are three hard X-ray beamlines at which crystallography can be performed: I711, I811 and I911. Beamline I711 is mainly used for powder diffraction. I811 is an EXAFS station at which surface XRD can also be carried out. I911 is a beamline with five experimental stations on a single superconducting wiggler source, of which two are currently used for macromolecular crystallography, namely the monochromatic station I911-2 and the tuneable station I911-3, which is equipped with a state-of-the-art goniometer and robotic sample changer. We will give an overview of the capabilities of these beamlines, focusing particularly on the macromolecular crystallography beamline I911 and some recent scientific highlights produced there. We will also give a brief overview of new beamlines for crystallography that are under construction or planned for the MAX IV facility.
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| 4. |
- Ursby, Thomas, et al.
(författare)
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BioMAX the first macromolecular crystallography beamline at MAX IV Laboratory
- 2020
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Ingår i: Journal of Synchrotron Radiation. - Chichester : Wiley-Blackwell. - 0909-0495 .- 1600-5775. ; 27, s. 1415-1429
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Tidskriftsartikel (refereegranskat)abstract
- BioMAX is the first macromolecular crystallography beamline at the MAX IV Laboratory 3 GeV storage ring, which is the first operational multi-bend achromat storage ring. Due to the low-emittance storage ring, BioMAX has a parallel, high-intensity X-ray beam, even when focused down to 20 μm × 5 μm using the bendable focusing mirrors. The beam is tunable in the energy range 5-25 keV using the in-vacuum undulator and the horizontally deflecting double-crystal monochromator. BioMAX is equipped with an MD3 diffractometer, an ISARA high-capacity sample changer and an EIGER 16M hybrid pixel detector. Data collection at BioMAX is controlled using the newly developed MXCuBE3 graphical user interface, and sample tracking is handled by ISPyB. The computing infrastructure includes data storage and processing both at MAX IV and the Lund University supercomputing center LUNARC. With state-of-the-art instrumentation, a high degree of automation, a user-friendly control system interface and remote operation, BioMAX provides an excellent facility for most macromolecular crystallography experiments. Serial crystallography using either a high-viscosity extruder injector or the MD3 as a fixed-target scanner is already implemented. The serial crystallography activities at MAX IV Laboratory will be further developed at the microfocus beamline MicroMAX, when it comes into operation in 2022. MicroMAX will have a 1 μm × 1 μm beam focus and a flux up to 1015 photons s with main applications in serial crystallography, room-temperature structure determinations and time-resolved experiments.
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| 5. |
- Bjelčić, Monika, et al.
(författare)
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Anaerobic fixed-target serial crystallography using sandwiched silicon nitride membranes
- 2023
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Ingår i: Acta Crystallographica Section D: Structural Biology. - 2059-7983. ; 79:Pt 11, s. 1018-1025
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Tidskriftsartikel (refereegranskat)abstract
- In recent years, the emergence of serial crystallography, initially pioneered at X-ray free-electron lasers (XFELs), has sparked a growing interest in collecting macromolecular crystallographic data at room temperature. Various fixed-target serial crystallography techniques have been developed, ranging from commercially available chips to in-house designs implemented at different synchrotron facilities. Nevertheless, there is currently no commercially available chip (known to the authors) specifically designed for the direct handling of oxygen-sensitive samples. This study presents a methodology employing silicon nitride chips arranged in a 'sandwich' configuration, enabling reliable room-temperature data collection from oxygen-sensitive samples. The method involves the utilization of a custom-made 3D-printed assembling tool and a MX sample holder. To validate the effectiveness of the proposed method, deoxyhemoglobin and methemoglobin samples were investigated using the BioMAX X-ray macromolecular crystallography beamline, the Balder X-ray absorption spectroscopy beamline and UV-Vis absorption spectroscopy.
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| 6. |
- Bjelčić, Monika, et al.
(författare)
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Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO
- 2024
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Ingår i: Acta Crystallographica Section F: Structural Biology Communications. - 2053-230X. ; 80:Pt 6, s. 117-124
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Tidskriftsartikel (refereegranskat)abstract
- Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 Å resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
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| 7. |
- Bjelčić, Monika, et al.
(författare)
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Room-temperature serial synchrotron crystallography structure of Spinacia oleracea RuBisCO
- 2024
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Ingår i: ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS. - 2053-230X. ; 80, s. 117-124
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Tidskriftsartikel (refereegranskat)abstract
- Ribulose-1,5-bisphosphate carboxylase/ oxygenase (RuBisCO) is the enzyme responsible for the first step of carbon dioxide (CO2) fixation in plants, which proceeds via the carboxylation of ribulose 1,5-biphosphate. Because of the enormous importance of this reaction in agriculture and the environment, there is considerable interest in the mechanism of fixation of CO2 by RuBisCO. Here, a serial synchrotron crystallography structure of spinach RuBisCO is reported at 2.3 angstrom resolution. This structure is consistent with earlier single-crystal X-ray structures of this enzyme and the results are a good starting point for a further push towards time-resolved serial synchrotron crystallography in order to better understand the mechanism of the reaction.
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| 8. |
- Bourgeois, D, et al.
(författare)
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A microspectrophotometer for UV-visible absorption and fluorescence studies of protein crystals
- 2002
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Ingår i: Journal of Applied Crystallography. - 1600-5767. ; 35, s. 319-326
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Tidskriftsartikel (refereegranskat)abstract
- Absorption microspectrophotometry has been shown to be of considerable help to probe crystalline proteins containing chromophores, metal centres, or coloured substrates/co-factors. Absorption spectra contribute to the proper interpretation of crystallographic structures, especially when transient intermediate states are studied. Here it is shown that fluorescence microspectrophotometry might also be used for such purposes if endogenous fluorophores are present in the macromolecule or when exogenous fluorophores are added and either bind to the protein or reside in the solvent channels. An off-line microspectrophotometer that is able to perform low-temperature absorption and fluorescence spectroscopy on crystals mounted in cryo-loops is described. One-shot steady-state emission spectra of outstanding quality were routinely collected from several samples. In some cases, crystals with optical densities that are too low or too high for absorption studies can still be tackled with fluorescence microspectrophotometry. The technique may be used for simple controls such as checking the presence, absence or redox state of a fluorescent substrate/co-factor. Potential applications in the field of kinetic crystallography are numerous. In addition, the possibility to probe key physico-chemical parameters of the crystal, such as temperature, pH or solvent viscosity, could trigger new studies in protein dynamics.
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| 9. |
- Cerenius, Yngve, et al.
(författare)
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Crystallography at MAX-lab
- 2004
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Ingår i: Synchrotron Radiation in Natural Science. - 1644-7190. ; 3:1-2, s. 13-16
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Tidskriftsartikel (refereegranskat)
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| 10. |
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| 11. |
- Gaponov, Yury, et al.
(författare)
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Some aspects of SR beamline alignment
- 2011
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Ingår i: Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment. - : Elsevier BV. - 0168-9002. ; 649:1, s. 231-233
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Konferensbidrag (refereegranskat)abstract
- Based on the Synchrotron Radiation (SR) beamline optical element-by-element alignment with analysis of the alignment results an optimized beamline alignment algorithm has been designed and developed. The alignment procedures have been designed and developed for the MAX-lab 1911-4 fixed energy beamline. It has been shown that the intermediate information received during the monochromator alignment stage can be used for the correction of both monochromator and mirror without the next stages of alignment of mirror, slits, sample holder, etc. Such an optimization of the beamline alignment procedures decreases the time necessary for the alignment and becomes useful and helpful in the case of any instability of the beamline optical elements, storage ring electron orbit or the wiggler insertion device. which could result in the instability of angular and positional parameters of the SR beam. A general purpose software package for manual, semi-automatic and automatic SR beamline alignment has been designed and developed using the developed algorithm. The TANGO control system is used as the middle-ware between the stand-alone beamline control applications BLTools, BPMonitor and the beamline equipment. (C) 2010 Elsevier B.V. All rights reserved.
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| 12. |
- Gogliettino, MA, et al.
(författare)
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The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the Archaeon Sulfolobus solfataricus
- 2004
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Ingår i: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 43:8, s. 2199-2208
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Tidskriftsartikel (refereegranskat)abstract
- We have examined and compared the effects of mutating Y41 and H155 in the iron superoxide dismutase (SOD) from the archaeon Sulfolobus solfataricus (Ss). These two neighboring residues in the active site are known to have crucial functions in structurally related SODs from different sources. The metal analysis indicates a slightly lower iron content after either Y41F or H155Q replacement, without any significant substitution of iron for manganese. The specific activity of SsSOD referred to the iron content is 17-fold reduced in the Y41F mutant, whereas it is less than 2-fold reduced by the H155Q mutation. The noticeable pH dependence of the activity of SsSOD and H155Q-SsSOD, due to the ionization of Y41 (pK 8.4), is lost in Y41F-SsSOD. After H155Q and even more after the Y41F substitution, the archaeal enzyme acquires a moderate sensitivity to sodium azide inhibition. The hydrogen peroxide inactivation of SsSOD is significantly increased after H155Q replacement; however, both mutants are insensitive to the modification of residue 41 by phenylmethanesulfonyl fluoride. Heat inactivation studies showed that the high stability of SsSOD is reduced by the H155Q mutation; hovewer, upon the addition of SDS, a much faster inactivation kinetics is observed both with wild-type and mutant SsSOD forms. The detergent is also required to follow thermal denaturation of the archaeal enzyme by Fourier transform infrared spectroscopy; these studies gave information about the effect of mutations and modification on flexibility and compactness of the protein structure. The crystal structure of Y41F mutant revealed an uninterrupted hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, which is not present in structures of the corresponding mutant SODs from other sources. These data suggest that Y41 and H155 are important for the structural and functional properties of SsSOD; in particular, Y41 seems to be a powerful regulator of the activity of SsSOD, whereas H155 is apparently involved in the organization of the active site of the enzyme.
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| 13. |
- Gorgisyan, Ishkhan, et al.
(författare)
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Fast, automated, continuous energy scans for experimental phasing at the BioMAX beamline
- 2023
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Ingår i: Journal of Synchrotron Radiation. - 0909-0495. ; 30, s. 885-894
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Tidskriftsartikel (refereegranskat)abstract
- In X-ray macromolecular crystallography (MX), single-wavelength anomalous dispersion (SAD) and multi-wavelength anomalous dispersion (MAD) techniques are commonly used for obtaining experimental phases. For an MX synchrotron beamline to support SAD and MAD techniques it is a prerequisite to have a reliable, fast and well automated energy scan routine. This work reports on a continuous energy scan procedure newly implemented at the BioMAX MX beamline at MAX IV Laboratory. The continuous energy scan is fully automated, capable of measuring accurate fluorescence counts over the absorption edge of interest while minimizing the sample exposure to X-rays, and is about a factor of five faster compared with a conventional step scan previously operational at BioMAX. The implementation of the continuous energy scan facilitates the prompt access to the anomalous scattering data, required for the SAD and MAD experiments.
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| 14. |
- Kristiansen, Paw, et al.
(författare)
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Vibrational stability of a cryocooled horizontal double-crystal monochromator
- 2016
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Ingår i: Journal of Synchrotron Radiation. - 1600-5775. ; 23:Pt 5, s. 1076-1081
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Tidskriftsartikel (refereegranskat)abstract
- The vibrational stability of a horizontally deflecting double-crystal monochromator (HDCM) is investigated. Inherently a HDCM will preserve the vertical beam stability better than a `normal' vertical double-crystal monochromator as the vibrations of a HDCM will almost exclusively affect the horizontal stability. Here both the relative pitch vibration between the first and second crystal and the absolute pitch vibration of the second crystal are measured. All reported measurements are obtained under active cooling by means of flowing liquid nitrogen (LN2). It is found that it is favorable to circulate the LN2 at high pressures and low flow rates (up to 5.9 bar and down to 3 l min(-1) is tested) to attain low vibrations. An absolute pitch stability of the second crystal of 18 nrad RMS, 2-2500 Hz, and a relative pitch stability between the two crystals of 25 nrad RMS, 1-2500 Hz, is obtained under cryocooling conditions that allow for 1516 W to be adsorbed by the LN2 before it vaporizes.
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| 15. |
- Mammen, C.B., et al.
(författare)
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Bent Diamond Crystals and Multilayer Based Optics at the new 5-Station Protein Crystallography Beamline ‘Cassiopeia’ at MAX-lab
- 2004
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Ingår i: AIP Conference Proceedings. - : AIP. - 0094-243X. - 0735401799 ; 705:1, s. 808-811
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Konferensbidrag (refereegranskat)abstract
- A new 5-station beamline for protein crystallography is being commissioned at the Swedish synchrotron light source MAX-II at Lund University. Of the 2K/gamma = 14 mrad horizontal wiggler fan, the central 2 mrad are used and split in three parts. The central 1 mrad will be used for a station optimized for MAD experiments and on each side of the central fan, from 0.5 mrad to 1 mrad, there are two fixed energy stations using different energies of the same part of the beam. These, in total five stations, can be used simultaneously and independently for diffraction data collection. The two upstream monochromators for the side stations are meridionally bent asymmetric diamond(111) crystals in Laue transmission geometry. The monochromators for the downstream side stations are bent Ge(111) crystals in asymmetric Bragg reflection geometry. Curved multilayer mirrors inserted in the monochromatic beams provide focusing in the vertical plane. The first side station is under commissioning, and a preliminary test protein data set has been collected. ©2004 American Institute of Physics
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| 16. |
- Mammen, C B, et al.
(författare)
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Design of a 5-station macromolecular crystallography beamline at MAX-Lab
- 2002
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Ingår i: Acta Physica Polonica. Series A: General Physics, Physics of Condensed Matter, Optics and Quantum Electronics, Atomic and Molecular Physics, Applied Physics. - 0587-4246. ; 101:5, s. 595-602
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Tidskriftsartikel (refereegranskat)abstract
- A beamline for macromolecular crystallography is under construction at the Swedish synchrotron light source MAX-lab at Lund University in a collaborative effort between Denmark and Sweden. Of the 7 mrad horizontal wiggler fan emitted from the new superconducting multipole wiggler, the central 2 mrad will be used and split in three parts. The central 1 mrad will be used for a tunable station optimised for multi-wavelength anomalous diffraction experiments and on each side of the central fan there will be two fixed wavelength stations using different energies of the same part of the beam. These in total five stations can be used simultaneously and independently for collecting diffraction data.
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| 17. |
- Shilova, Anastasiia, et al.
(författare)
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Current status and future opportunities for serial crystallography at MAX IV Laboratory
- 2020
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Ingår i: Journal of Synchrotron Radiation. - Chichester : Wiley-Blackwell. - 0909-0495 .- 1600-5775. ; 27, s. 1095-1102
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Tidskriftsartikel (refereegranskat)abstract
- Over the last decade, serial crystallography, a method to collect complete diffraction datasets from a large number of microcrystals delivered and exposed to an X-ray beam in random orientations at room temperature, has been successfully implemented at X-ray free-electron lasers and synchrotron radiation facility beamlines. This development relies on a growing variety of sample presentation methods, including different fixed target supports, injection methods using gas-dynamic virtual-nozzle injectors and high-viscosity extrusion injectors, and acoustic levitation of droplets, each with unique requirements. In comparison with X-ray free-electron lasers, increased beam time availability makes synchrotron facilities very attractive to perform serial synchrotron X-ray crystallography (SSX) experiments. Within this work, the possibilities to perform SSX at BioMAX, the first macromolecular crystallography beamline at studies from the SSX user program: an implementation of a high-viscosity extrusion injector to perform room temperature serial crystallography at BioMAX using two solid supports - silicon nitride membranes (Silson, UK) and XtalTool (Jena Bioscience, Germany). Future perspectives for the dedicated serial crystallography beamline MicroMAX at MAX IV Laboratory, which will provide parallel and intense micrometre-sized X-ray beams, are discussed.
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| 18. |
- Thunnissen, Marjolein, et al.
(författare)
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BioMAX: The Future Macromolecular Crystallography Beamline at MAX IV
- 2013
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Ingår i: 11th International Conference on Synchrotron Radiation Instrumentation (SRI 2012). - : IOP Publishing. - 1742-6596 .- 1742-6588. ; 425
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Konferensbidrag (refereegranskat)abstract
- This paper describes the preliminary design of the BioMAX beamline at the 3 GeV ring of the MAX IV facility, focusing on the optics and x-ray beam performance. The MAX IV facility will include two storage rings with 1.5 GeV and 3.0 GeV electron energy and a linac serving both as injector for the two rings and feeding a short pulse facility. BioMAX is one of the first seven beamlines funded at the MAX IV facility. It is a multipurpose high-throughput beamline for macromolecular crystallography. The beamline aims to be robust and simple to operate with a beam benefiting from the properties of the MAX IV 3 GeV ring. However it does not aim at the smallest beam or crystal sizes since it is foreseen that it will be complemented with a microfocus beamline aiming at a beam size of 1 mu m. The beamline experiment setup will be highly automated, both in terms of sample handling hardware and data analysis, including feedback to the data collection. The BioMAX beamline is planned to be in operation in 2016.
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| 19. |
- Ursby, Thomas
(författare)
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From Time-Averaged to Time-Resolved Crystallography: Studies on Superoxide Dismutase and Myoglobin
- 1998
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- We have studied protein motions with nanosecond time-resolved crystallography. The release of carbon monoxide from its complex with myoglobin (MbCO) was triggered by nanosecond laser pulses. X-ray data were collected with time delays ranging from 4 ns to 1.9 ms using the Laue method, at the European Synchrotron Radiation Facility in Grenoble. For the first time point, X-ray pulses of 150 ps duration were used. Electron difference maps show the release of the CO and the subsequent motion of the iron out of the haem plane. In the 4 ns difference map, a positive density feature is found at a position coinciding with that of an intermediate docking site seen at low temperature. The following time points show the rebinding of the CO, and also indications of protein relaxations extending further than 4 ns. This is the first time-resolved protein crystallography experiment with nanosecond time-resolution yielding structural results. We have developed instrumentation and methods for time-resolved protein crystallography, including a method to reduce the noise in electron density difference maps from poorly accurate data. The method is also applicable to other cases where the signal to noise ratio is low. The crystal structure of iron superoxide dismutase (SOD) from the hyperthermophilic archaeon Sulfolobus solfataricus has been determined to 2.3 Å resolution by molecular replacement. The structure revealed an increased number of inter-subunit ion-pairs in a compact tetramer. We suggest this to be important for the thermostability. However, the general fold is found to be similar to other known iron- or manganese SOD structures. In addition, the electron density maps revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site.
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| 20. |
- Ursby, Thomas, et al.
(författare)
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Iron superoxide dismutase from the archaeon Sulfolobus sulfataricus : Analysis of structure and thermostability.
- 1999
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Ingår i: Journal of Molecular Biology. - : Elsevier BV. - 1089-8638 .- 0022-2836. ; 286:1, s. 189-205
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Tidskriftsartikel (refereegranskat)abstract
- The crystal structure of superoxide dismutase (SOD) from the hyper thermophile Sulfolobus solfataricus has been determined at 2.3 Å resolution by molecular replacement and refined to a crystallographic R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group C2 (a = 76.3 Å, b = 124.3 Å,c = 60.3 Å, β = 128.8°) with two identical monomers in the asymmetric unit. The monomer has a molecular weight of 24 kDa and consists of 210 amino acid residues of which 205 are visible in the electron density map. The overall fold of the monomer of S. solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S. solfataricus SOD forms a very compact tetramer of a type similar to that of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show an elevated number of inter-subunit ion-pairs compared with the mesophilic SOD from Mycobacterium tuberculosis and the thermophilic SOD from Thermus thermophilus. However, in contrast to the A. pyrophilus SOD structure, the number of intra-subunit ion-pairs as well as inter-subunit hydrogen bonds is not higher than in the compared mesophilic and thermophilic SOD structures. The electron density also revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site. Its involvement in the specific activity of the enzyme is discussed.
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| 21. |
- Ursby, Thomas, et al.
(författare)
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The macromolecular crystallography beamline I911-3 at the MAX IV laboratory.
- 2013
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Ingår i: Journal of Synchrotron Radiation. - 1600-5775. ; 20:Pt 4, s. 648-653
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Tidskriftsartikel (refereegranskat)abstract
- The macromolecular crystallography beamline I911-3, part of the Cassiopeia/I911 suite of beamlines, is based on a superconducting wiggler at the MAX II ring of the MAX IV Laboratory in Lund, Sweden. The beamline is energy-tunable within a range between 6 and 18 keV. I911-3 opened for users in 2005. In 2010-2011 the experimental station was completely rebuilt and refurbished such that it has become a state-of-the-art experimental station with better possibilities for rapid throughput, crystal screening and work with smaller samples. This paper describes the complete I911-3 beamline and how it is embedded in the Cassiopeia suite of beamlines.
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| 22. |
- Ursby, Thomas, et al.
(författare)
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The new macromolecular crystallography stations at MAX-lab: The MAD station
- 2004
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Ingår i: AIP Conference Proceedings. - 0094-243X .- 1551-7616. ; 705, s. 1241-1244
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Konferensbidrag (refereegranskat)abstract
- A new beamline, Cassiopeia, at MAX II is about to come into operation. It consists of an energy-tunable station and four side stations intended for macromolecular crystallography. The X-ray source is a 3.5 T superconducting multipole wiggler installed in the 1.5 GeV MAX II storage ring. The energy-tunable station use grazing incidence Rh-coated silicon mirrors and an internally water-cooled Si(111) double-crystal monochromator while the four side stations use bent diamond and germanium monochromators and multilayer mirrors. This paper concentrates on the optics design of the energy-tunable station and also briefly describes other beamline components
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