Crystallization and preliminary X-ray diffraction analysis of an active-site mutant of 'loopless' family GH19 chitinase from Bryum coronatum in a complex with chitotetraose

Takayuki Ohnuma, Naoyuki Umemoto, Toki Taira, Tamo Fukamizo, Tomoyuki Numata

研究成果: Contribution to journalArticle査読

2 被引用数 (Scopus)

抄録

The catalytic mechanism of family GH19 chitinases is not well understood owing to insufficient information regarding the three-dimensional structures of enzyme-substrate complexes. Here, the crystallization and preliminary X-ray diffraction analysis of a selenomethionine-labelled active-site mutant of 'loopless' family GH19 chitinase from the moss Bryum coronatum in complex with chitotetraose, (GlcNAc)4, are reported. The crystals were grown using the vapour-diffusion method. They diffracted to 1.58Å resolution using synchrotron radiation at the Photon Factory. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 74.5, b = 58.4, c = 48.1Å, β = 115.6°. The asymmetric unit of the crystals is expected to contain one protein molecule, with a Matthews coefficient of 2.08Å3Da-1 and a solvent content of 41%.

本文言語英語
ページ(範囲)1360-1362
ページ数3
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
69
12
DOI
出版ステータス出版済み - 12 2013
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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