Purification and crystallization of the human EF-hand tumour suppressor protein S100A2
- Fachbereich Biologie, Universität Konstanz, Postfach M665, Universitätsstrasse 10, 78457 Konstanz (Germany)
- Swiss Light Source at Paul Scherrer Insitute, 5232 Villigen PSI (Switzerland)
Human recombinant tumour suppressor S100A2 and a mutant lacking cysteine residues have been purified and crystallized. Only the crystals of the mutant protein diffracted to appropriate resolution and a complete data set was recorded at 1.7 Å. S100A2 is a Ca{sup 2+}-binding EF-hand protein that is mainly localized in the nucleus. There, it acts as a tumour suppressor by binding and activating p53. Wild-type S100A2 and a S100A2 variant lacking cysteines have been purified. CD spectroscopy showed that there are no changes in secondary-structure composition. The S100A2 mutant was crystallized in a calcium-free form. The crystals, with dimensions 30 × 30 × 70 µm, diffract to 1.7 Å and belong to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 43.5, b = 57.8, c = 59.8 Å, α = β = γ = 90°. Preliminary analysis of the X-ray data indicates that there are two subunits per asymmetric unit.
- OSTI ID:
- 22356400
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 11; Other Information: PMCID: PMC2225223; PMID: 17077493; PUBLISHER-ID: ll5085; OAI: oai:pubmedcentral.nih.gov:2225223; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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