Purification, crystallization and preliminary X-ray diffraction studies on human Ca2+-binding protein S100B.

Thorsten Ostendorp; Claus W Heizmann; Peter M H Kroneck; Günter Fritz

doi:10.1107/s1744309105018014

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Purification, crystallization and preliminary X-ray diffraction studies on human Ca2+-binding protein S100B.

Thorsten Ostendorp·Claus W Heizmann·Peter M H Kroneck·Günter Fritz

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Abstract

S100B, a Ca2+-binding protein, acts intracellularly as a Ca2+-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 Ca2+-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 A and belong to space group P2(1), with unit-cell parameters a = 63.4, b = 81.6, c = 71.5 A, alpha = 90, beta = 107, gamma = 90 degrees. Preliminary analysis of the X-ray data indicate that there are four homodimers per asymmetric unit.

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Calcium Cloning, Molecular Crystallography, X-Ray Cytokines DNA, Complementary Dimerization Escherichia coli Humans Magnetic Resonance Spectroscopy Nerve Growth Factors Protein Conformation Recombinant Proteins S100 Calcium Binding Protein beta Subunit S100 Proteins X-Ray Diffraction X-Rays Journal Article Research Support, Non-U.S. Gov't

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Thorsten Ostendorp, Claus W Heizmann, Peter M H Kroneck, Günter Fritz. 2005-06-15. Purification, crystallization and preliminary X-ray diffraction studies on human Ca2+-binding protein S100B.. https://doi.org/10.1107/s1744309105018014

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