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Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv.

ABSTRACT: Full-length GroEL1 from Mycobacterium tuberculosis H37Rv was cloned, overexpressed and purified. Crystals were obtained by the hanging-drop vapor-diffusion method and contained a 23 kDa GroEL1 fragment. A complete native data set was collected from a single frozen crystal that belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 75.47, b = 78.67, c = 34.89 A, alpha = beta = gamma = 90 degrees , and diffracted to 2.2 A resolution on a home X-ray source.

SUBMITTER: Sielaff B

PROVIDER: S-EPMC2852334 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv.

Sielaff Bernhard B Lee Ki Seog KS Tsai Francis T F FT

Acta crystallographica. Section F, Structural biology and crystallization communications 20100331 Pt 4

Full-length GroEL1 from Mycobacterium tuberculosis H37Rv was cloned, overexpressed and purified. Crystals were obtained by the hanging-drop vapor-diffusion method and contained a 23 kDa GroEL1 fragment. A complete native data set was collected from a single frozen crystal that belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 75.47, b = 78.67, c = 34.89 A, alpha = beta = gamma = 90 degrees , and diffracted to 2.2 A resolution on a home X-ray source. ...[more]

PMID: 20383012

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