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http://purl.uniprot.org/citations/15272186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15272186http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15272186http://www.w3.org/2000/01/rdf-schema#comment"An alkaline mannanase (EC 3.2.1.78) from the alkaliphilic Bacillus sp. strain JAMB-602 was cloned and sequenced. The deduced amino-acid sequence of the enzyme suggested that the enzyme consists of a catalytic and unknown additional domains. The recombinant enzyme expressed by B. subtilis was crystallized using the hanging-drop vapour-diffusion method at 277 K. X-ray diffraction data were collected to 1.65 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 70.7, b = 79.5, c = 80.4 A. The asymmetric unit contains one protein molecule, with a corresponding VM of 2.26 A3 Da(-1) and a solvent content of 45.6%. Molecular replacement for initial phasing was carried out using the three-dimensional structure of a mannanase from Thermomonospora fusca as a search model, which corresponds to the catalytic domain of the alkaline mannanase. It gave sufficient phases to build the unknown domain."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.org/dc/terms/identifier"doi:10.1107/S0907444904014313"xsd:string
http://purl.uniprot.org/citations/15272186http://purl.org/dc/terms/identifier"doi:10.1107/s0907444904014313"xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Hatada Y."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Hatada Y."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Horikoshi K."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Horikoshi K."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Ito S."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Sakai H."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Takeda N."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Takeda N."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Akita M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Akita M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Kawamoto M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Kawamoto M."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Grant W.D."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Grant W.D."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Hirasawa K."xsd:string
http://purl.uniprot.org/citations/15272186http://purl.uniprot.org/core/author"Hirasawa K."xsd:string