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Publication Abstract from PubMed

Structural genomics discovery projects require ready access to both X-ray diffraction and NMR spectroscopy 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 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 multi acre synchrotron facilities for data collection. In this paper we report on the development and use of 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.

X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source.,Abendroth J, McCormick MS, Edwards TE, Staker B, Loewen R, Gifford M, Rifkin J, Mayer C, Guo W, Zhang Y, Myler P, Kelley A, Analau E, Hewitt SN, Napuli AJ, Kuhn P, Ruth RD, Stewart LJ J Struct Funct Genomics. 2010 Mar;11(1):91-100. Epub 2010 Apr 3. PMID:20364333^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.