X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source

• Published in: Journal of structural and functional genomics Vol. 11; no. 1; pp. 91 - 100
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: Dordrecht Dordrecht : Springer Netherlands 01.03.2010; Springer Netherlands; Springer Nature B.V
• Subjects: Amino Acid Oxidoreductases; Biochemistry; Bioinformatics; Biomedical and Life Sciences; Carrier Proteins; Crystallography; Crystals; Data collection; Design; Forestry Management; Genomics; Glycine Decarboxylase Complex H-Protein; Human Genetics; Infectious diseases; Laboratories; Lasers; Life Sciences; Light; Microbial Genetics and Genomics; Multienzyme Complexes; Muramidase; Mycobacterium tuberculosis; Mycobacterium tuberculosis - chemistry; Plant Genetics and Genomics; Proteins; Proteins - chemistry; Radiation; Synchrotrons; Transferases; Tuberculosis; X-Ray Diffraction - instrumentation; X-Ray Diffraction - methods; X-Rays; Compact light source; X-ray crystallography; Inverse Compton
• ISSN: 1345-711X; 1570-0267
• DOI: 10.1007/s10969-010-9087-6

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.