Purification, crystallization and preliminary X-ray diffraction studies of a Ca2+-binding protein, human S100P

Acta Crystallographica. Section D, Biological Crystallography
Hongmei ZhangZihe Rao

Abstract

S100P, a Ca(2+)-binding protein, is a member of the S100 family. Its presence is associated with the development of prostate cancer, but its cellular function is not known. Recombinant human S100P has been expressed and purified in bacterial cells and crystals of human S100P in the calcium-bound state have been grown using the vapour-diffusion technique with PEG 4000 as precipitant. Diffraction data have been obtained to a resolution of 2.0 A from a single frozen S100P crystal which belongs to the space group P4(1)2(1)2, with unit-cell parameters a = b = 60.8, c = 47.6 A.

Citations

Feb 16, 2010·Amino Acids·Adriana GibadulinovaSilvia Pastorekova
Jan 1, 2003·Journal of Molecular Biology·Hongmei ZhangZihe Rao
Mar 21, 2012·Proceedings of the National Academy of Sciences of the United States of America·Michael WaisbergSusan K Pierce
Jul 1, 2009·International Journal of Molecular Sciences·Liefeng ZhangYong Ren

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