Purification, crystallization and preliminary X-ray diffraction studies of a Ca2+-binding protein, human S100P.
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.
Zhang
Hongmei
H
Laboratory of Structural Biology and MOE Laboratory of Protein Science, School of Life Science and Engineering, Tsinghua University, Beijing 100084, People's Republic of China.
Wang
Zhilong
Z
Ding
Yi
Y
Wang
Guozhen
G
Wang
Xiaodong
X
Gao
Feng
F
Tang
Hong
H
Barraclough
Roger
R
Rudland
Philip S
PS
Rao
Zihe
Z
D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D006801:Humans; D009363:Neoplasm Proteins; D014961:X-Ray Diffraction
D002135:Calcium-Binding Proteins; D009363:Neoplasm Proteins; C103003:S100P protein, human