Purification, crystallization and preliminary X-ray analysis of human pirin.
Pirin is a novel highly conserved nuclear protein, but very little is known about its cellular function. Human pirin has been cloned, expressed, purified and crystallized using PEG as precipitant. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 67.0, c = 107.3 A, alpha = beta = gamma = 90 A. It contains one molecule per asymmetric unit and diffracts to 2.0 A under cryoconditions (100 K) using an in-house Cu rotating-anode X-ray generator.
Zeng
Q
Q
Department of Biological Science and Technology, Tsinghua University, Beijing 100084, People's Republic of China.
Li
X
X
Bartlam
M
M
Wang
G
G
Pang
H
H
Rao
Z
Z
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D003461:Crystallography; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D049308:Dioxygenases; D004926:Escherichia coli / Q000378:metabolism; D005615:Freezing; D015723:Gene Library; D006801:Humans; D008099:Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D013696:Temperature; D014965:X-Rays
D002352:Carrier Proteins; D018076:DNA, Complementary; D009687:Nuclear Proteins; D049308:Dioxygenases; C105340:PIR protein, human