3IFT

Crystal structure of glycine cleavage system protein H from Mycobacterium tuberculosis, using X-rays from the Compact Light Source.

Summary for 3IFT

• Entry DOI: 10.2210/pdb3ift/pdb
• Related: 3hgb
• Descriptor: Glycine cleavage system H protein (2 entities in total)
• Functional Keywords: niaid, decode, uw, sbri, glycine cleavage system, structural genomics, psi-2, protein structure initiative, accelerated technologies center for gene to 3d structure, atcg3d, seattle structural genomics center for infectious disease, lipoyl, methylamine binding protein, oxidoreductase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 15244.58

Authors

Edwards, T.E.,Abendroth, J.,Staker, B.,Mayer, C.,Phan, I.,Kelley, A.,Analau, E.,Leibly, D.,Rifkin, J.,Loewen, R.,Ruth, R.D.,Stewart, L.J.,Accelerated Technologies Center for Gene to 3D Structure (ATCG3D) (deposition date: 2009-07-25, release date: 2009-08-11, Last modification date: 2023-09-06)

Primary citation

Abendroth, J.,McCormick, M.S.,Edwards, T.E.,Staker, B.,Loewen, R.,Gifford, M.,Rifkin, J.,Mayer, C.,Guo, W.,Zhang, Y.,Myler, P.,Kelley, A.,Analau, E.,Hewitt, S.N.,Napuli, A.J.,Kuhn, P.,Ruth, R.D.,Stewart, L.J.
X-ray structure determination of the glycine cleavage system protein H of Mycobacterium tuberculosis using an inverse Compton synchrotron X-ray source.
J.Struct.Funct.Genom., 11:91-100, 2010

PubMed 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.

PubMed: 20364333
DOI: 10.1007/s10969-010-9087-6

Experimental method

X-RAY DIFFRACTION (2 Å)