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 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
Cite this
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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 journal › Article
TY - JOUR
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.
UR - http://www.scopus.com/inward/record.url?scp=0345876937&partnerID=8YFLogxK
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M3 - Article
VL - 6
SP - 399
EP - 402
JO - Protein and Peptide Letters
JF - Protein and Peptide Letters
SN - 0929-8665
IS - 6
ER -