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PMID: 16754987 Published · ppublish English

Purification, crystallization and preliminary X-ray analysis of Mycobacterium tuberculosisfolylpolyglutamate synthase (MtbFPGS).

Acta crystallographica. Section F, Structural biology and crystallization communications ·Vol. 62 ·No. Pt 6 ·2006-08-04

Young P G, Smith C A, Sun X, Baker E N, Metcalf P

Abstract

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 CoCl2 or by vapour diffusion in the presence of ADP, dihydrofolate and CaCl2. X-ray diffraction data to approximately 2.0 and 2.6 A 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(1)3, with a unit-cell parameter of 112.6 and 111.8 A, respectively. Structure determination is proceeding.

Article Info
Journal
Acta crystallographica. Section F, Structural biology and crystallization communications
Abbr.
Acta Crystallogr Sect F Struct Biol Cryst Commun
ISSN
1744-3091
Published
2006-08-04
Indexed
2006-06-06
Updated
2014-09-09
Language
English
Country/Region
England
NLM ID
101226117
External Links
PubMed source
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