Crystallization and preliminary X-ray crystallographic analysis of rat calcineurin B homologous protein 1.
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin, potentially modulating their function. CHP1 has been crystallized at 277 K using polyethylene glycol as a precipitant. The crystal belongs to space group P2(1), with unit-cell parameters a = 55.5, b = 38.5, c = 90.0 A, beta = 90.7 degrees. A full set of diffraction data was collected to 2.2 A resolution at 100 K using the Photon Factory synchrotron-radiation source.
Naoe
Youichi
Y
International Graduate School of Arts and Sciences, Yokohama City University, Yokohama 230-0045, Japan.
Arita
Kyouhei
K
Hashimoto
Hiroshi
H
Kanazawa
Hiroshi
H
Sato
Mamoru
M
Shimizu
Toshiyuki
T
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D004926:Escherichia coli / Q000235:genetics; D008074:Lipoproteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011092:Polyethylene Glycols; D051381:Rats; D014835:Volatilization; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D002135:Calcium-Binding Proteins; D008074:Lipoproteins; C098929:calcium binding protein p22, rat; D011092:Polyethylene Glycols