Volume 58, Issue 4 pp. 694-696

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

First published: 16 June 2004
Zihe Rao, e-mail: [email protected]

Abstract

S100P, a Ca2+-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 Å from a single frozen S100P crystal which belongs to the space group P41212, with unit-cell parameters a = b = 60.8, c = 47.6 Å.

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