title: X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source.
abstract: 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.
authors.affiliation: Emerald BioStructures, 7869 NE Day Road West, Bainbridge Island, WA 98110, USA.
authors.forename: Jan
authors.initials: J
authors.lastname: Abendroth
authors.forename: Michael S
authors.initials: MS
authors.lastname: McCormick
authors.forename: Thomas E
authors.initials: TE
authors.lastname: Edwards
authors.forename: Bart
authors.initials: B
authors.lastname: Staker
authors.forename: Roderick
authors.initials: R
authors.lastname: Loewen
authors.forename: Martin
authors.initials: M
authors.lastname: Gifford
authors.forename: Jeff
authors.initials: J
authors.lastname: Rifkin
authors.forename: Chad
authors.initials: C
authors.lastname: Mayer
authors.forename: Wenjin
authors.initials: W
authors.lastname: Guo
authors.forename: Yang
authors.initials: Y
authors.lastname: Zhang
authors.forename: Peter
authors.initials: P
authors.lastname: Myler
authors.forename: Angela
authors.initials: A
authors.lastname: Kelley
authors.forename: Erwin
authors.initials: E
authors.lastname: Analau
authors.forename: Stephen Nakazawa
authors.initials: SN
authors.lastname: Hewitt
authors.forename: Alberto J
authors.initials: AJ
authors.lastname: Napuli
authors.forename: Peter
authors.initials: P
authors.lastname: Kuhn
authors.forename: Ronald D
authors.initials: RD
authors.lastname: Ruth
authors.forename: Lance J
authors.initials: LJ
authors.lastname: Stewart
mesh_terms: D000594:Amino Acid Oxidoreductases; D002352:Carrier Proteins; D050961:Glycine Decarboxylase Complex H-Protein; D009097:Multienzyme Complexes; D009113:Muramidase; D009169:Mycobacterium tuberculosis / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D017356:Synchrotrons; D014166:Transferases; D014961:X-Ray Diffraction / Q000295:instrumentation / Q000379:methods*; D014965:X-Rays
chemical_list: D002352:Carrier Proteins; D050961:Glycine Decarboxylase Complex H-Protein; D009097:Multienzyme Complexes; D011506:Proteins; C064525:glycine cleavage system; D000594:Amino Acid Oxidoreductases; D014166:Transferases; C421864:hen egg lysozyme; D009113:Muramidase