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

Takashi Kumasaka, Hiroyuki Takeya, Masaki Yamamoto, Yoshio Yamakawa, Tamotsu Omori-satoh, Hideaki Moriyama, Nobuo Tanaka, Mamoru Sato, Yukiteru Katsube, Sadaaki Iwanaga

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


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

Original languageEnglish (US)
Pages (from-to)929-930
Number of pages2
JournalJournal of Biochemistry
Issue number5
StatePublished - May 1995
Externally publishedYes


  • Crystallization
  • Metalloproteinase
  • Snake venom
  • X-ray diffraction

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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