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- aggregation classification "A1".
- aggregation creator B510275.
- aggregation creator B510276.
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- aggregation date "2010".
- aggregation format "application/pdf".
- aggregation hasFormat 912420.bibtex.
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- aggregation isPartOf urn:issn:1744-3091.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda".
- aggregation abstract "Disaccharide phosphorylases are able to catalyze both the synthesis and the breakdown of disaccharides and have thus emerged as attractive platforms for tailor-made sugar synthesis. Cellobiose phosphorylase from Cellulomonas uda (CPCuda) is an enzyme that belongs to glycoside hydrolase family 94 and catalyzes the reversible breakdown of cellobiose [beta-d-glucopyranosyl-(1,4)-D-glucopyranose] to alpha-D-glucose-1-phosphate and D-glucose. Crystals of ligand-free recombinant CPCuda and of its complexes with substrates and reaction products yielded complete X-ray diffraction data sets to high resolution using synchrotron radiation but suffered from significant variability in diffraction quality. In at least one case an intriguing space-group transition from a primitive monoclinic to a primitive orthorhombic lattice was observed during data collection. The structure of CPCuda was determined by maximum-likelihood molecular replacement, thus establishing a starting point for an investigation of the structural and mechanistic determinants of disaccharide phosphorylase activity.".
- aggregation authorList BK855355.
- aggregation endPage "351".
- aggregation issue "3".
- aggregation startPage "346".
- aggregation volume "66".
- aggregation aggregates 912431.
- aggregation isDescribedBy 912420.
- aggregation similarTo S1744309110002642.
- aggregation similarTo LU-912420.