Purification, crystallization and preliminary X-ray diffraction studies on human Ca{sup 2+}-binding protein S100B
- Fachbereich Biologie, Universität Konstanz, Postfach M665, Universitätsstrasse 10, 78467 Konstanz (Germany)
- Division of Clinical Chemistry and Biochemistry, Department of Pediatrics, University of Zürich, Steinwiesstrasse 75, 8032 Zürich (Switzerland)
Human recombinant EF-hand Ca{sup 2+}-binding protein S100B has been purified and crystallized. A complete data set was recorded to 1.9 Å. S100B, a Ca{sup 2+}-binding protein, acts intracellularly as a Ca{sup 2+}-signalling protein but is also secreted to the extracellular space, acting in a cytokine-like manner through its receptor RAGE. Recombinant human S100B has been purified and crystallized in the Ca{sup 2+}-bound state. Size-exclusion chromatography indicates that S100B can exist as a dimer and as a multimer in solution. Crystals of S100B diffract to 1.9 Å and belong to space group P2{sub 1}, with unit-cell parameters a = 63.4, b = 81.6, c = 71.5 Å, α = 90, β = 107, γ = 90°. Preliminary analysis of the X-ray data indicate that there are four homodimers per asymmetric unit.
- OSTI ID:
- 22356153
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 7; Other Information: PMCID: PMC1952468; PMID: 16511125; PUBLISHER-ID: gx5048; OAI: oai:pubmedcentral.nih.gov:1952468; 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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