Work

Purification, crystallization and preliminary X-ray analysis ofMycobacterium tuberculosisfolylpolyglutamate synthase (MtbFPGS)

Year: 2006

Type: article

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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309106017180

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

Institutions: University of Auckland, Stanford Synchrotron Radiation Lightsource

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

OpenAlex ID: W1966415675

FWCI: 0.651

Cites: 12

Cited by: 6

Related to: 10