title: Crystallization and preliminary crystallographic study of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp).
abstract: The plant phospholipase D (PLD) is considered to be a key enzyme involved in various physiological processes such as signal transduction and membrane metabolism. Crystals of the PLD protein from Vigna unguiculata have been produced from the recombinant 768 amino-acid protein. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 157.7, b = 65.6, c = 90.2 A, beta = 111.5 degrees. There is one molecule in the asymmetric unit. Frozen crystals diffract to at least 1.94 A resolution using synchrotron radiation. A search for heavy-atom derivatives using ytterbium and tungstate is currently under way in order to solve the three-dimensional structure.
authors.affiliation: Information Génétique et Structurale, UMR1889 CNRS-AVENTIS, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France. chantal@igs.cnrs-mrs.fr
authors.forename: C
authors.initials: C
authors.lastname: Abergel
authors.forename: A
authors.initials: A
authors.lastname: Abousalham
authors.forename: S
authors.initials: S
authors.lastname: Chenivesse
authors.forename: M
authors.initials: M
authors.lastname: Rivière
authors.forename: A M
authors.initials: AM
authors.lastname: Moustacas-Gardies
authors.forename: R
authors.initials: R
authors.lastname: Verger
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010739:Phospholipase D / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D019685:Rosales / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D010739:Phospholipase D