Abstract
The catalytic domain of an alkaline beta-mannanase from the alkaliphilic Bacillus sp. N16-5 has been expressed and purified. The recombinant enzyme was crystallized using the hanging-drop vapour-diffusion method at 298 K. X-ray diffraction data were collected to 1.6 A resolution. The crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 59.03, b = 63.31, c = 83.34 A. Initial phasing was carried out by molecular replacement using the three-dimensional structure of a mannanase from the alkaliphilic Bacillus sp. JAMB602 as a search model.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus / enzymology
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Sequence
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Crystallization
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DNA Primers
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DNA, Bacterial / genetics
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Fungal Proteins / chemistry
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Fungal Proteins / metabolism
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Hydrogen-Ion Concentration
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Plant Proteins / chemistry
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Plant Proteins / metabolism
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Plasmids
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X-Ray Diffraction / methods
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beta-Mannosidase / chemistry*
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beta-Mannosidase / genetics
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beta-Mannosidase / metabolism*
Substances
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Bacterial Proteins
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DNA Primers
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DNA, Bacterial
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Fungal Proteins
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Plant Proteins
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beta-Mannosidase