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Purification and crystallization of the human EF-hand tumour suppressor protein S100A2.

ABSTRACT: S100A2 is a Ca(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 x 30 x 70 microm, diffract to 1.7 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 43.5, b = 57.8, c = 59.8 A, alpha = beta = gamma = 90 degrees. Preliminary analysis of the X-ray data indicates that there are two subunits per asymmetric unit.

SUBMITTER: Koch M

PROVIDER: S-EPMC2225223 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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Purification and crystallization of the human EF-hand tumour suppressor protein S100A2.

Koch Michael M Diez Joachim J Fritz Günter G

Acta crystallographica. Section F, Structural biology and crystallization communications 20061020 Pt 11

S100A2 is a Ca(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 x 30 x 70 microm, diffract to 1.7 A and belong to space group P2(1)2(1)2(1), with unit-cell pa ...[more]

PMID: 17077493

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