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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Cloning, purification, crystallization and preliminary crystallographic analysis of human phosphoglycerate mutase. Wang, Y., Cheng, Z., Liu, L., Wei, Z., Wan, M., Gong, W. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
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