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

doi:10.1093/oxfordjournals.jbchem.a124820

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 journal › Article › peer-review

1 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	929-930
Number of pages	2
Journal	Journal of Biochemistry
Volume	117
Issue number	5
DOIs	https://doi.org/10.1093/oxfordjournals.jbchem.a124820
State	Published - May 1995
Externally published	Yes

Keywords

Crystallization
Metalloproteinase
Snake venom
X-ray diffraction

ASJC Scopus subject areas

General Medicine

Access to Document

10.1093/oxfordjournals.jbchem.a124820

Cite this

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title = "Crystallization and preliminary X-ray study of H2-proteinase from the venom of Trimeresurus flavoviridis",

abstract = "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 {\aa} and c = 82.3 {\aa}. The asymmetric unit contains one protein molecule. Diffraction data for a native crystal were collected up to 2.0 {\aa} resolution",

keywords = "Crystallization, Metalloproteinase, Snake venom, X-ray diffraction",

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

year = "1995",

month = may,

doi = "10.1093/oxfordjournals.jbchem.a124820",

language = "English (US)",

volume = "117",

pages = "929--930",

journal = "Journal of Biochemistry",

issn = "0021-924X",

publisher = "Oxford University Press",

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T1 - Crystallization and preliminary X-ray study of H2-proteinase from the venom of Trimeresurus flavoviridis

AU - Kumasaka, Takashi

AU - Takeya, Hiroyuki

AU - Yamamoto, Masaki

AU - Yamakawa, Yoshio

AU - Omori-satoh, Tamotsu

AU - Moriyama, Hideaki

AU - Tanaka, Nobuo

AU - Sato, Mamoru

AU - Katsube, Yukiteru

AU - Iwanaga, Sadaaki

PY - 1995/5

Y1 - 1995/5

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AB - 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

KW - Crystallization

KW - Metalloproteinase

KW - Snake venom

KW - X-ray diffraction

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