Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1
- International Graduate School of Arts and Sciences, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045 (Japan)
- Department of Biological Science, Graduate School of Science, Osaka University, Machikaneyama-cho 1-16, Toyonaka, Osaka 560-0043 (Japan)
Calcineurin B homologous protein 1 from rat was expressed in E. coli, purified and crystallized. A full set of X-ray diffraction data has been collected to 2.2 Å resolution using a synchrotron-radiation source. Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na{sup +}/H{sup +} exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function. CHP1 has been crystallized at 277 K using polyethylene glycol as a precipitant. The crystal belongs to space group P2{sub 1}, with unit-cell parameters a = 55.5, b = 38.5, c = 90.0 Å, β = 90.7°. A full set of diffraction data was collected to 2.2 Å resolution at 100 K using the Photon Factory synchrotron-radiation source.
- OSTI ID:
- 22356025
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 6; Other Information: PMCID: PMC1952330; PMID: 16511110; PUBLISHER-ID: vr5033; OAI: oai:pubmedcentral.nih.gov:1952330; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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