4zb5 | pdb_00004zb5

A form of glucose isomerase collected at 100K.

spinqualitylabelsall models 4zb5, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zb5 is a 1 chain structure with sequence from "actinomyces_rubiginosus"_preobrazhenskaya_et_al._in_gauze_et_al._1957 "actinomyces rubiginosus" preobrazhenskaya et al. in gauze et al. 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLC, MN Related: 4zbo, 4zb2 Gene: xylA ("Actinomyces rubiginosus" Preobrazhenskaya et al. in Gauze et al. 1957) Activity: Xylose isomerase, with EC number 5.3.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [XYLA_STRRU] Involved in D-xylose catabolism. Publication Abstract from PubMed Dehydration may change the crystal lattice and affect the mosaicity, resolution and quality of X-ray diffraction data. A dehydrating environment can be generated around a crystal in several ways with various degrees of precision and complexity. This study uses a high-precision crystal humidifier/dehumidifier to provide an airstream of known relative humidity in which the crystals are mounted: a precise yet hassle-free approach to altering crystal hydration. A protocol is introduced to assess the impact of crystal dehydration systematically applied to nine experimental crystal systems. In one case, that of glucose isomerase, dehydration triggering a change of space group from I222 to P21212 was observed. This observation is supported by an extended study of the behaviour of the glucose isomerase crystal structure during crystal dehydration. A generic protocol for protein crystal dehydration using the HC1b humidity controller.,Lobley CM, Sandy J, Sanchez-Weatherby J, Mazzorana M, Krojer T, Nowak RP, Sorensen TL Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):629-40. doi:, 10.1107/S2059798316003065. Epub 2016 Apr 26. PMID:27139626 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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