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  • Title: 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.
    Author: Ohnuma T, Umemoto N, Taira T, Fukamizo T, Numata T.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2013 Dec; 69(Pt 12):1360-2. PubMed ID: 24316830.
    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 1.58 Å 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 = 48.1 Å, β = 115.6°. The asymmetric unit of the crystals is expected to contain one protein molecule, with a Matthews coefficient of 2.08 Å(3) Da(-1) and a solvent content of 41%.
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