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4US6

New Crystal Form of Glucose Isomerase Grown in Short Peptide Supramolecular Hydrogels

Summary for 4US6
Entry DOI10.2210/pdb4us6/pdb
DescriptorXYLOSE ISOMERASE, CALCIUM ION, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsisomerase, new polymorph
Biological sourceSTREPTOMYCES RUBIGINOSUS
Cellular locationCytoplasm: P24300
Total number of polymer chains2
Total formula weight87318.21
Authors
Gavira, J.A.,Conejero-Muriel, M.,Diaz-Mochon, J.J.,Alvarez de Cienfuegos, L. (deposition date: 2014-07-03, release date: 2015-05-13, Last modification date: 2024-01-10)
Primary citationConejero-Muriel, M.,Gavira, J.A.,Pineda-Molina, E.,Belsom, A.,Bradley, M.,Moral, M.,Garcia-Lopez Duran, J.D.D.,Luque Gonzalez, A.,Diaz-Mochon, J.J.,Contreras-Montoya, R.,Martinez-Peragon, A.,Cuerva, J.M.,Alvarez De Cienfuegos, L.
Influence of the Chirality of Short Peptide Supramolecular Hydrogels in Protein Crystallogenesis.
Chem.Commun.(Camb.), 51:3862-, 2015
Cited by
PubMed Abstract: For the first time the influence of the chirality of the gel fibers in protein crystallogenesis has been studied. Enantiomeric hydrogels 1 and 2 were tested with model proteins lysozyme and glucose isomerase and a formamidase extracted from B. cereus. Crystallization behaviour and crystal quality of these proteins in both hydrogels are presented and compared.
PubMed: 25655841
DOI: 10.1039/C4CC09024A
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.2 Å)
Structure validation

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