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Purification, crystallization and preliminary X-ray analysis of Hsp33 from Saccharomyces cerevisiae.

ABSTRACT: The heat-shock protein Hsp33 from the yeast Saccharomyces cerevisiae has been overexpressed, purified and crystallized. A crystal was obtained using the hanging-drop vapour-diffusion method and a data set was collected to 2.7 A resolution. The crystal belongs to space group P4(3)2(1)2, with unit-cell parameters a = b = 96.43, c = 132.22 A, alpha = beta = gamma = 90 degrees . The asymmetric unit is assumed to contain two subunits of Hsp33, with a V(M) value of 2.96 A(3) Da(-1) and a solvent content of 58.41%.

SUBMITTER: Liu W

PROVIDER: S-EPMC2330124 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray analysis of Hsp33 from Saccharomyces cerevisiae.

Liu Wei W Zhou Ye-Yun YY Teng Mai-Kun MK Zhou Cong-Zhao CZ

Acta crystallographica. Section F, Structural biology and crystallization communications 20070117 Pt 2

The heat-shock protein Hsp33 from the yeast Saccharomyces cerevisiae has been overexpressed, purified and crystallized. A crystal was obtained using the hanging-drop vapour-diffusion method and a data set was collected to 2.7 A resolution. The crystal belongs to space group P4(3)2(1)2, with unit-cell parameters a = b = 96.43, c = 132.22 A, alpha = beta = gamma = 90 degrees . The asymmetric unit is assumed to contain two subunits of Hsp33, with a V(M) value of 2.96 A(3) Da(-1) and a solvent conte ...[more]

PMID: 17277453

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