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

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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%.

Original languageEnglish
Pages (from-to)1360-1362
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number12
DOIs
Publication statusPublished - Dec 1 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

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

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