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Cloning, purification, crystallization and preliminary crystallographic analysis of human phosphoglycerate mutase
Yanli Wang1, Zhongjun Cheng, Lin Liu
1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Abstract:
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.
