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Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase
J Cherfils1, R Rosa, M C Garel
1Laboratoire de Biologie Physicochimique, CNRS UA1131, Université Paris-Sud, Orsay, France.
Journal of Molecular Biology
|March 20, 1991
Abstract:
Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100.4 A and alpha = beta = gamma = 81.2 degrees. The asymmetric unit contains either a dimeric enzyme molecule, or a monomer.