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Title: Purification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosis folylpolyglutamate synthase (MtbFPGS)

Journal Article · · Acta Crystallographica. Section F
 [1];  [2]; ;  [3]
  1. Stanford Synchrotron Radiation Laboratory, MS 992575 Sand Hill Road, Menlo Park, CA 94025 (United States)
  2. HortResearch Palmerston North, Tennent Drive, Private Bag 11 030, Palmerston North (New Zealand)
  3. Laboratory of Structural Biology, School of Biological Sciences, Thomas Building, 3A Symonds Street, Auckland (New Zealand)

The gene encoding M. tuberculosis FPGS (MtbFPGS; Rv2447c) has been cloned and the protein has been expressed in E. coli. The purified protein was crystallized and X-ray diffraction data were collected to 2.0 Å resolution. The gene encoding Mycobacterium tuberculosis FPGS (MtbFPGS; Rv2447c) has been cloned and the protein (51 kDa) expressed in Escherichia coli. The purified protein was crystallized either by the batch method in the presence of adenosine diphosphate (ADP) and CoCl{sub 2} or by vapour diffusion in the presence of ADP, dihydrofolate and CaCl{sub 2}. X-ray diffraction data to approximately 2.0 and 2.6 Å resolution were collected at the Stanford Synchrotron Radiation Laboratory (SSRL) for crystals grown under the respective conditions. Both crystals belong to the cubic space group P2{sub 1}3, with a unit-cell parameter of 112.6 and 111.8 Å, respectively. Structure determination is proceeding.

OSTI ID:
22360220
Journal Information:
Acta Crystallographica. Section F, Vol. 62, Issue Pt 6; Other Information: PMCID: PMC2243083; PMID: 16754987; PUBLISHER-ID: bw5148; OAI: oai:pubmedcentral.nih.gov:2243083; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English