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

ABSTRACT: 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(1)2(1)2, with two molecules per asymmetric unit which are related by translational symmetry.

SUBMITTER: Hatzopoulos GN

PROVIDER: S-EPMC2330178 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature

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

Hatzopoulos Georgios N GN Mueller-Dieckmann Jochen J

Acta crystallographica. Section F, Structural biology and crystallization communications 20070210 Pt 3

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(1)2(1)2, with two molecules per asymmetric unit which are related by translational symmetry. ...[more]

PMID: 17329809

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