Crystallization and preliminary X-ray study of H2-proteinase from the venom of Trimeresurus flavoviridis

• Published in: Journal of biochemistry (Tokyo) Vol. 117; no. 5; p. 929
• Main Authors: Kumasaka, T, Takeya, H, Yamamoto, M, Yamakawa, Y, Omori-Satoh, T, Moriyama, H, Tanaka, N, Sato, M, Katsube, Y, Iwanaga, S
• Format: Journal Article
• Language: English
• Published: England 01-05-1995
• Subjects: Animals; Crotalid Venoms - enzymology; Crystallization; Metalloendopeptidases - chemistry; Trimeresurus; X-Ray Diffraction
• ISSN: 0021-924X
• DOI: 10.1093/oxfordjournals.jbchem.a124820

H2-proteinase, a non-hemorrhagic metalloproteinase from the venom of Trimeresurus flavoviridis, has been crystallized by vapor diffusion from solutions containing ammonium sulfate. The crystals belong to the tetragonal space group, P41212 or P43212, with unit cell dimensions of a = b = 77.8 A and c = 82.3 A. The asymmetric unit contains one protein molecule. Diffraction data for a native crystal were collected up to 2.0 A resolution.