Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of initiation factor 1 from Mycobacterium tuberculosis

Journal Article · Thu Mar 01 00:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910700437X· OSTI ID:22360277

Hatzopoulos, Georgios N.; Mueller-Dieckmann, Jochen ^[1]

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1. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg (Germany)

Initiation factor 1 from M. tuberculosis was cloned, expressed, purified and crystallized. A complete data set has been collected to 1.47 Å resolution. Initiation factor 1 (IF-1; Rv3462c) from Mycobacterium tuberculosis, a component of the 30S initiation complex, was cloned and heterologously expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and crystallized. A complete data set has been collected to high resolution. The crystals belonged to space group P2{sub 1}2{sub 1}2, with two molecules per asymmetric unit which are related by translational symmetry.

• OSTI ID: 22360277
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 3; Other Information: PMCID: PMC2330178; PMID: 17329809; PUBLISHER-ID: en5218; OAI: oai:pubmedcentral.nih.gov:2330178; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CRYSTALLIZATION
CRYSTALS
ESCHERICHIA COLI
MOLECULES
PROTEINS
RESOLUTION
SPACE GROUPS
SYMMETRY