title: Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase.
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.
authors.affiliation: Laboratoire de Biologie Physicochimique, CNRS UA1131, Université Paris-Sud, Orsay, France.
authors.forename: J
authors.initials: J
authors.lastname: Cherfils
authors.forename: R
authors.initials: R
authors.lastname: Rosa
authors.forename: M C
authors.initials: MC
authors.lastname: Garel
authors.forename: M C
authors.initials: MC
authors.lastname: Calvin
authors.forename: J
authors.initials: J
authors.lastname: Rosa
authors.forename: J
authors.initials: J
authors.lastname: Janin
mesh_terms: D001731:Bisphosphoglycerate Mutase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003460:Crystallization; D004912:Erythrocytes / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006801:Humans; D014961:X-Ray Diffraction
chemical_list: D001731:Bisphosphoglycerate Mutase