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Sökning: onr:"swepub:oai:lup.lub.lu.se:2e450b0b-7ac5-46c2-add0-89a50c0b160d" > Microgravity crysta...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003771naa a2200361 4500
001oai:lup.lub.lu.se:2e450b0b-7ac5-46c2-add0-89a50c0b160d
003SwePub
008220705s2022 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/2e450b0b-7ac5-46c2-add0-89a50c0b160d2 URI
0247 a https://doi.org/10.1038/s41526-022-00199-32 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Drago, Victoria N.u University of Toledo4 aut
2451 0a Microgravity crystallization of perdeuterated tryptophan synthase for neutron diffraction
264 c 2022-05-04
264 1b Springer Science and Business Media LLC,c 2022
520 a Biologically active vitamin B6-derivative pyridoxal 5′-phosphate (PLP) is an essential cofactor in amino acid metabolic pathways. PLP-dependent enzymes catalyze a multitude of chemical reactions but, how reaction diversity of PLP-dependent enzymes is achieved is still not well understood. Such comprehension requires atomic-level structural studies of PLP-dependent enzymes. Neutron diffraction affords the ability to directly observe hydrogen positions and therefore assign protonation states to the PLP cofactor and key active site residues. The low fluxes of neutron beamlines require large crystals (≥0.5 mm3). Tryptophan synthase (TS), a Fold Type II PLP-dependent enzyme, crystallizes in unit gravity with inclusions and high mosaicity, resulting in poor diffraction. Microgravity offers the opportunity to grow large, well-ordered crystals by reducing gravity-driven convection currents that impede crystal growth. We developed the Toledo Crystallization Box (TCB), a membrane-barrier capillary-dialysis device, to grow neutron diffraction-quality crystals of perdeuterated TS in microgravity. Here, we present the design of the TCB and its implementation on Center for Advancement of Science in Space (CASIS) supported International Space Station (ISS) Missions Protein Crystal Growth (PCG)-8 and PCG-15. The TCB demonstrated the ability to improve X-ray diffraction and mosaicity on PCG-8. In comparison to ground control crystals of the same size, microgravity-grown crystals from PCG-15 produced higher quality neutron diffraction data. Neutron diffraction data to a resolution of 2.1 Å has been collected using microgravity-grown perdeuterated TS crystals from PCG-15.
650 7a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng
7001 a Devos, Juliette M.u Institut Laue Langevin4 aut
7001 a Blakeley, Matthew P.u Institut Laue Langevin4 aut
7001 a Forsyth, V. Trevoru Lund University,Lunds universitet,LINXS - Institute of advanced Neutron and X-ray Science,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Molekylär Biofysik,Forskargrupper vid Lunds universitet,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Molecular Biophysics,Lund University Research Groups,Keele University,Institut Laue Langevin4 aut0 (Swepub:lu)tr2830fo
7001 a Kovalevsky, Andrey Y.u Oak Ridge National Laboratory4 aut
7001 a Schall, Constance A.u University of Toledo4 aut
7001 a Mueser, Timothy C.u University of Toledo4 aut
7102 a University of Toledob Institut Laue Langevin4 org
7730 t npj Microgravityd : Springer Science and Business Media LLCg 8:1q 8:1x 2373-8065
8564 u http://dx.doi.org/10.1038/s41526-022-00199-3x freey FULLTEXT
8564 8u https://lup.lub.lu.se/record/2e450b0b-7ac5-46c2-add0-89a50c0b160d
8564 8u https://doi.org/10.1038/s41526-022-00199-3

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