Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12

Takuo Matsumoto; Takamasa Nonaka; Haruhiko Katouda; Masayuki Hashimoto; Takeshi Watanabe; Yukio Mitsui

Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12

Takuo Matsumoto, Takamasa Nonaka, Haruhiko Katouda, Masayuki Hashimoto, Takeshi Watanabe, Yukio Mitsui

Institute of Molecular Medicine

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

The catalytic domain of chitinase A1 from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. The crystals belong to the triclinic space group P1 with cell dimensions a = 43.96Å, b = 48.62Å, c = 54.59Å, α =108.90°, β= 95.06°, and γ = 115.77°, and contain one molecule in the asymmetric unit. High-quality diffraction data were collected at 20°C with radiation from a synchrotron source up to 1.5Å resolution.

Original language	English
Pages (from-to)	399-402
Number of pages	4
Journal	Protein and Peptide Letters
Volume	6
Issue number	6
Publication status	Published - 1999 Dec 1

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry

Cite this

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title = "Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12",

abstract = "The catalytic domain of chitinase A1 from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. The crystals belong to the triclinic space group P1 with cell dimensions a = 43.96{\AA}, b = 48.62{\AA}, c = 54.59{\AA}, α =108.90°, β= 95.06°, and γ = 115.77°, and contain one molecule in the asymmetric unit. High-quality diffraction data were collected at 20°C with radiation from a synchrotron source up to 1.5{\AA} resolution.",

author = "Takuo Matsumoto and Takamasa Nonaka and Haruhiko Katouda and Masayuki Hashimoto and Takeshi Watanabe and Yukio Mitsui",

year = "1999",

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T1 - Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12

AU - Matsumoto, Takuo

AU - Nonaka, Takamasa

AU - Katouda, Haruhiko

AU - Hashimoto, Masayuki

AU - Watanabe, Takeshi

AU - Mitsui, Yukio

PY - 1999/12/1

Y1 - 1999/12/1

N2 - The catalytic domain of chitinase A1 from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. The crystals belong to the triclinic space group P1 with cell dimensions a = 43.96Å, b = 48.62Å, c = 54.59Å, α =108.90°, β= 95.06°, and γ = 115.77°, and contain one molecule in the asymmetric unit. High-quality diffraction data were collected at 20°C with radiation from a synchrotron source up to 1.5Å resolution.

AB - The catalytic domain of chitinase A1 from Bacillus circulans WL-12 was crystallized by vapor-diffusion technique. The crystals belong to the triclinic space group P1 with cell dimensions a = 43.96Å, b = 48.62Å, c = 54.59Å, α =108.90°, β= 95.06°, and γ = 115.77°, and contain one molecule in the asymmetric unit. High-quality diffraction data were collected at 20°C with radiation from a synchrotron source up to 1.5Å resolution.

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JO - Protein and Peptide Letters

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SN - 0929-8665

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ER -

Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12

Abstract

All Science Journal Classification (ASJC) codes

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