Cloning, purification, crystallization and preliminary crystallographic analysis of human phosphoglycerate mutase.
Human B-type 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (dPGM-B) has been cloned, overexpressed and purified, with a yield of 30% of the total protein. Crystals of human dPGM-B were obtained using the hanging-drop vapour-diffusion technique. X-ray diffraction data were collected to 2.8 A resolution. The human dPGM-B crystals belong to space group P2(1), with unit-cell parameters a = 130.5, b = 75.9, c = 187.0 A, beta = 94.4 degrees. There could be between 9 and 18 monomers per asymmetric unit, with 12 molecules being the most likely.
Wang
Yanli
Y
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Cheng
Zhongjun
Z
Liu
Lin
L
Wei
Zhiyi
Z
Wan
Mao
M
Gong
Weimin
W
D001921:Brain / Q000378:metabolism; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods*; D018076:DNA, Complementary / Q000378:metabolism; D015723:Gene Library; D006801:Humans; D010736:Phosphoglycerate Mutase / Q000737:chemistry* / Q000235:genetics*; D014961:X-Ray Diffraction
D018076:DNA, Complementary; D010736:Phosphoglycerate Mutase