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Crystallization and preliminary crystallographic analysis of ?-mannanase from Bacillus licheniformis.

ABSTRACT: The mannan endo-1,4-?-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, ? = 98.29°, and showed diffraction to 2.3?Å resolution.

SUBMITTER: Songsiriritthigul C 

PROVIDER: S-EPMC3034611 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic analysis of β-mannanase from Bacillus licheniformis.

Songsiriritthigul Chomphunuch C   Lapboonrueng Sasithorn S   Roytrakul Sittiruk S   Haltrich Dietmar D   Yamabhai Montarop M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110122 Pt 2

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 mole  ...[more]

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