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Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda

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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.
Keywords
ENZYMES, GLUCOSE, VIBRIO-PROTEOLYTICUS, CHITOBIOSE PHOSPHORYLASE, CELLVIBRIO, REACTION-MECHANISM, CRYSTALS, SOFTWARE

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MLA
Van Hoorebeke, Annelies et al. “Crystallization and X-ray Diffraction Studies of Cellobiose Phosphorylase from Cellulomonas Uda.” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 66.3 (2010): 346–351. Print.
APA
Van Hoorebeke, A., Stout, J., Kyndt, J., De Groeve, M., Dix, I., Desmet, T., Soetaert, W., et al. (2010). Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 66(3), 346–351.
Chicago author-date
Van Hoorebeke, Annelies, Jan Stout, John Kyndt, Manu De Groeve, Ina Dix, Tom Desmet, Wim Soetaert, Jozef Van Beeumen, and Savvas Savvides. 2010. “Crystallization and X-ray Diffraction Studies of Cellobiose Phosphorylase from Cellulomonas Uda.” Acta Crystallographica Section F-structural Biology and Crystallization Communications 66 (3): 346–351.
Chicago author-date (all authors)
Van Hoorebeke, Annelies, Jan Stout, John Kyndt, Manu De Groeve, Ina Dix, Tom Desmet, Wim Soetaert, Jozef Van Beeumen, and Savvas Savvides. 2010. “Crystallization and X-ray Diffraction Studies of Cellobiose Phosphorylase from Cellulomonas Uda.” Acta Crystallographica Section F-structural Biology and Crystallization Communications 66 (3): 346–351.
Vancouver
1.
Van Hoorebeke A, Stout J, Kyndt J, De Groeve M, Dix I, Desmet T, et al. Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. 2010;66(3):346–51.
IEEE
[1]
A. Van Hoorebeke et al., “Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda,” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, vol. 66, no. 3, pp. 346–351, 2010.
@article{912420,
  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.},
  author       = {Van Hoorebeke, Annelies and Stout, Jan and Kyndt, John and De Groeve, Manu and Dix, Ina and Desmet, Tom and Soetaert, Wim and Van Beeumen, Jozef and Savvides, Savvas},
  issn         = {1744-3091},
  journal      = {ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS},
  keywords     = {ENZYMES,GLUCOSE,VIBRIO-PROTEOLYTICUS,CHITOBIOSE PHOSPHORYLASE,CELLVIBRIO,REACTION-MECHANISM,CRYSTALS,SOFTWARE},
  language     = {eng},
  number       = {3},
  pages        = {346--351},
  title        = {Crystallization and X-ray diffraction studies of cellobiose phosphorylase from Cellulomonas uda},
  url          = {http://dx.doi.org/10.1107/S1744309110002642},
  volume       = {66},
  year         = {2010},
}

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