title: Crystallization and preliminary crystallographic analysis of β-mannanase from Bacillus licheniformis.
abstract: The mannan endo-1,4-β-mannosidase (ManB) from Bacillus licheniformis strain DSM13 was overexpressed in Escherichia coli. Purification of the thermostable and alkali-stable recombinant mannanase yielded approximately 50 mg enzyme per litre of culture. Crystals were grown by hanging-drop vapour diffusion using a precipitant solution consisting of 12%(w/v) PEG 8000, 0.2 M magnesium acetate tetrahydrate and 0.1 M MES pH 6.5. The protein crystallized in the monoclinic space group P2(1), with two molecules per asymmetric unit and unit-cell parameters a = 48.58, b = 91.75, c = 89.55 Å, β = 98.29°, and showed diffraction to 2.3 Å resolution.
authors.affiliation: Synchrotron Light Research Institute, Nakhon Ratchasima, Thailand. chomphunuch@slri.or.th
authors.forename: Chomphunuch
authors.initials: C
authors.lastname: Songsiriritthigul
authors.forename: Sasithorn
authors.initials: S
authors.lastname: Lapboonrueng
authors.forename: Sittiruk
authors.initials: S
authors.lastname: Roytrakul
authors.forename: Dietmar
authors.initials: D
authors.lastname: Haltrich
authors.forename: Montarop
authors.initials: M
authors.lastname: Yamabhai
mesh_terms: D001407:Bacillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004058:Diffusion; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D044902:beta-Mannosidase / Q000737:chemistry* / Q000235:genetics
chemical_list: D011994:Recombinant Proteins; D044902:beta-Mannosidase