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

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)399-402
Number of pages4
JournalProtein and Peptide Letters
Volume6
Issue number6
Publication statusPublished - 1999 Dec 1

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Chitinases
Synchrotrons
Bacilli
Crystallization
Bacillus
Catalytic Domain
Diffraction
Vapors
Radiation
Crystals
Molecules
Data Accuracy

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry

Cite this

Matsumoto, Takuo ; Nonaka, Takamasa ; Katouda, Haruhiko ; Hashimoto, Masayuki ; Watanabe, Takeshi ; Mitsui, Yukio. / Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12. In: Protein and Peptide Letters. 1999 ; Vol. 6, No. 6. pp. 399-402.
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Crystallization and apreliminary crystallographic analysis of the catalytic domain of chitinase A1 from Bacillus circulans WL-12. / Matsumoto, Takuo; Nonaka, Takamasa; Katouda, Haruhiko; Hashimoto, Masayuki; Watanabe, Takeshi; Mitsui, Yukio.

In: Protein and Peptide Letters, Vol. 6, No. 6, 01.12.1999, p. 399-402.

Research output: Contribution to journalArticle

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