X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source.
X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source.
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DOI:
10.1007/s10969-010-9087-6
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发表时间:
2010-03
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影响因子:
--
通讯作者:
Stewart, Lance J
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文献类型:
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作者:
Abendroth, Jan;McCormick, Michael S;Edwards, Thomas E;Staker, Bart;Loewen, Roderick;Gifford, Martin;Rifkin, Jeff;Mayer, Chad;Guo, Wenjin;Zhang, Yang;Myler, Peter;Kelley, Angela;Analau, Erwin;Hewitt, Stephen Nakazawa;Napuli, Alberto J;Kuhn, Peter;Ruth, Ronald D;Stewart, Lance J
Structural genomics discovery projects require ready access to both X-ray and NMR instrumentation which support the collection of experimental data needed to solve large numbers of novel protein structures. The most productive X-ray crystal structure determination laboratories make extensive frequent use of tunable synchrotron X-ray light to solve novel structures by anomalous diffraction methods. This requires that frozen cryo-protected crystals be shipped to large government-run synchrotron facilities for data collection. In an effort to eliminate the need to ship crystals for data collection, we have developed the first laboratory-scale synchrotron light source capable of performing many of the state-of-the-art synchrotron applications in X-ray science. This Compact Light Source is a first-in-class device that uses inverse Compton scattering to generate X-rays of sufficient flux, tunable wavelength and beam size to allow high-resolution X-ray diffraction data collection from protein crystals. We report on benchmarking tests of X-ray diffraction data collection with hen egg white lysozyme, and the successful high-resolution X-ray structure determination of the Glycine cleavage system protein H from Mycobacterium tuberculosis using diffraction data collected with the Compact Light Source X-ray beam.