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

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

DOI:https://doi.org/10.1107/S1744309107000681· OSTI ID:22360260

Liu, Wei; Zhou, Ye-Yun; Teng, Mai-Kun; Zhou, Cong-Zhao ^[1]

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1. Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027 (China)

Heat-shock protein Hsp33 from S. cerevisiae was crystallized and diffraction data were collected to 2.7 Å resolution. 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 Å resolution. The crystal belongs to space group P4{sub 3}2{sub 1}2, with unit-cell parameters a = b = 96.43, c = 132.22 Å, α = β = γ = 90°. The asymmetric unit is assumed to contain two subunits of Hsp33, with a V{sub M} value of 2.96 Å{sup 3} Da{sup −1} and a solvent content of 58.41%.

• OSTI ID: 22360260
• Journal Information: Acta Crystallographica. Section F, Vol. 63, Issue Pt 2; Other Information: PMCID: PMC2330124; PMID: 17277453; PUBLISHER-ID: fw5121; OAI: oai:pubmedcentral.nih.gov:2330124; 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
CRYSTALLIZATION
CRYSTALS
DIFFRACTION
DIFFUSION
RESOLUTION
SOLVENTS
SPACE GROUPS