Cloning, purification, crystallization and preliminary crystallographic analysis of human phosphoglycerate mutase.

Acta Crystallogr D Biol Crystallogr

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.

Published: October 2004

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.

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http://dx.doi.org/10.1107/S0907444904018967DOI Listing

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