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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Thorsten OstendorpGunter Fritz

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.

References

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Oct 3, 1998·Acta Crystallographica. Section D, Biological Crystallography·A T BrüngerG L Warren
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Sep 1, 2004·Biochemical and Biophysical Research Communications·Ingo MarenholzGünter Fritz

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Citations

Dec 29, 2009·The Journal of Biological Chemistry·Shangwei HouToshinori Hoshi
Aug 24, 2007·Journal of Molecular Modeling·Artur GieldonRebecca Del Conte
Mar 6, 2008·Molecular Nutrition & Food Research·Timo M BuetlerThierry Delatour
May 7, 2015·Acta Crystallographica. Section D, Biological Crystallography·Jaime L JensenChristopher L Colbert
Aug 26, 2018·Journal of Neurochemistry·Fabrizio MichettiMaria Concetta Geloso
Jul 31, 2007·The EMBO Journal·Thorsten OstendorpGünter Fritz
Feb 28, 2008·The Prostate·Edith Uetz-von AllmenDaniel F Legler
Oct 7, 2006·Journal of Leukocyte Biology·Roberta BianchiRosario Donato
Oct 16, 2010·Structure·Michael KochGünter Fritz

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