Purification and crystallization of the human EF-hand tumour suppressor protein S100A2.
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.
Koch
Michael
M
Fachbereich Biologie, Universität Konstanz, Postfach M665, Universitätsstrasse 10, 78457 Konstanz, Germany.
Diez
Joachim
J
Fritz
Günter
G
D002630:Chemotactic Factors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization; D018076:DNA, Complementary; D006801:Humans; D017433:Protein Structure, Secondary; D021122:Protein Subunits / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D009418:S100 Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D002630:Chemotactic Factors; D018076:DNA, Complementary; D021122:Protein Subunits; D011994:Recombinant Proteins; D009418:S100 Proteins; C098997:S100A2 protein, human