期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 67, 期 -, 页码 217-220出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110049067
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资金
- Synchrotron Light Research Institute [1-2551/LS02]
The mannan endo-1,4-beta-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 angstrom, beta = 98.29 degrees, and showed diffraction to 2.3 angstrom resolution.
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