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- Butorin, SM, et al.
(författare)
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Resonant photoemission from vanadium compounds with excitation near V 2p threshold
- 1999
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Ingår i: JOURNAL OF ELECTRON SPECTROSCOPY AND RELATED PHENOMENA. - : ELSEVIER SCIENCE BV. - 0368-2048. ; 103, s. 739-743
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Valence-band photoemission measurements were performed on VC0.80, VN0.89, VF3, and VF2+x at various photon energies across V 2p absorption edges. While on-resonance spectra of VC0.80 and VN0.89 are dominated by V LW Auger lines, strongly resonating struct
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- Buyanova, Irina A, et al.
(författare)
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Effect of high-temperature electron irradiation on the formation of radiative defects in silicon
- 1999
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Ingår i: Physica. B, Condensed matter. - 0921-4526 .- 1873-2135. ; 274, s. 528-531
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Tidskriftsartikel (refereegranskat)abstract
- Defect formation processes in silicon caused by electron irradiation performed at elevated temperatures are studied in detail using photoluminescence (PL) spectroscopy. The use of high temperature during electron irradiation has been found to affect considerably the defect formation process, In particular, several new unknown excitonic PL lines were discovered in carbon-rich Si wafers subjected to electron irradiation at temperatures higher than 450 degrees C, The dominant new luminescent center gives rise to a bound exciton PL emission at 0.961 eV. The center is shown to be efficiently created by electron irradiation at temperatures from 450 degrees C up to 600 degrees C. The electronic structure of the 0.961 eV PL center can be described as a pseudodonor case, where the hole is strongly bound at a level 187 meV above the valence band, while the electron is a effective-mass-like particle weakly bound by approximate to 21 meV in the BE state, (C) 1999 Elsevier Science B.V. All rights reserved.
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- Jansson, Magnus, et al.
(författare)
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High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli.
- 1996
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Ingår i: Journal of Biomolecular NMR. - 0925-2738 .- 1573-5001. ; 7:2, s. 131-41
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Tidskriftsartikel (refereegranskat)abstract
- An approach to produce 13C- and 15N-enriched proteins is described. The concept is based on intracellular production of the recombinant proteins in Escherichia coli as fusions to an IgG-binding domain, Z, derived from staphylococcal protein A. The production method provides yields of 40-200 mg/l of isotope-enriched fusion proteins in defined minimal media. In addition, the Z fusion partner facilitates the first purification step by IgG affinity chromatography. The production system is applied to isotope enrichment of human insulin-like growth factor II (IGF-II), bovine pancreatic trypsin inhibitor (BPTI), and Z itself. High levels of protein production are achieved in shaker flasks using totally defined minimal medium supplemented with 13C(6)-glucose and (15NH4)2SO4 as the only carbon and nitrogen sources. Growth conditions were optimized to obtain high protein production levels and high levels of isotope incorporation, while minimizing 13C(6)-glucose usage. Incorporation levels of 13C and/or 15N isotopes in purifies IGF-II, BPTI, and Z were confirmed using mass spectrometry and NMR spectroscopy. More than 99% of total isotope enrichment was obtained using a defined isotope-enriched minimal medium. The optimized systems provide reliable, high-level production of isotope-enriched fusion proteins. They can be used to produce 20-40 mg/l of properly folded Z and BPTI proteins. The production system of recombinant BPTI is state-of-the-art and provides the highest known yield of native refolded BPTI.
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