Crystallization and preliminary X-ray diffraction studies of Streptomyces phospholipase A2 in a calcium-binding form.
Phospholipase A2 (PLA2) as a calcium-binding form, produced by Streptomyces violaceoruber, was crystallized in a form suitable for the diffraction analysis using the vapor diffusion method. Crystals were grown in 0.1 M Tris-HCl buffer (pH 8.5), 20 mM Ca2+ containing 50-60% (v/v) 2-methyl-2,4-pentanediol as a precipitant. They belong to the monoclinic space group P2(1), with the cell dimensions a=38.3 A, b=54.3 A, c=30.6 A, and beta=90.2 degrees. The crystals diffract the X-ray well and the diffraction intensity data were collected up to 1.6 A resolution. The crystal volume per unit mass, V(M) is 2.35 A3 Da(-1) with one molecule in the asymmetric unit, which corresponds to a solvent content of 47.7%.
Matoba
Y
Y
Institute of Pharmaceutical Sciences, Faculty of Medicine, Hiroshima University, Japan.
Kumagai
T
T
Sugiyama
M
M
D002118:Calcium / Q000378:metabolism; D003460:Crystallization; D010741:Phospholipases A / Q000737:chemistry* / Q000378:metabolism; D054467:Phospholipases A2; D013302:Streptomyces / Q000201:enzymology*; D014961:X-Ray Diffraction
D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium