Crystallization and Preliminary X-Ray Study of H2-Proteinase from the Venom of Trimeresurus flavoviridis

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 Å and c...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 1995-05, Vol.117 (5), p.929-930
Main Authors: Kumasaka, Takashi, Takeya, Hiroyuki, Yamamoto, Masaki, Yamakawa, Yoshio, Omori-Satoh, Tamotsu, Moriyama, Hideaki, Tanaka, Nobuo, Sato, Mamoru, Katsube, Yukiteru, Iwanaga, Sadaaki
Format: Article
Language:English
Subjects:
Animals
Crotalid Venoms - enzymology
Crystallization
Metalloendopeptidases - chemistry
metalloproteinase
snake venom
Trimeresurus
X-Ray Diffraction
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Summary: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 Å and c = 82.3 Å. The asymmetric unit contains one protein molecule. Diffraction data for a native crystal were collected up to 2.0 Å resolution
ISSN:0021-924X
1756-2651
DOI:10.1093/oxfordjournals.jbchem.a124820