Crystallization and preliminary crystallographic study of a recombinant phospholipase D from cowpea (Vigna unguiculata L. Walp).
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.
Abergel
C
C
Information Génétique et Structurale, UMR1889 CNRS-AVENTIS, 31 Chemin Joseph Aiguier, 13402 Marseille CEDEX 20, France. chantal@igs.cnrs-mrs.fr
Abousalham
A
A
Chenivesse
S
S
Rivière
M
M
Moustacas-Gardies
A M
AM
Verger
R
R
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*
D011994:Recombinant Proteins; D010739:Phospholipase D