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 i n various physiological processes such as signal transduction and membrane metabolism. Crystals of the PLD protein from Vigna unguiculata have been pr oduced 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 Angstrom, beta = 111.5 degrees. There is one molecule in the as ymmetric unit. Frozen crystals diffract to at least 1.94 Angstrom resolutio n using synchrotron radiation. A search for heavy-atom derivatives using yt terbium and tungstate is currently under way in order to solve the three-di mensional structure.