Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lobley CM, Sandy J, Sanchez-Weatherby J, Mazzorana M, Krojer T, Nowak RP, Sorensen TL. A generic protocol for protein crystal dehydration using the HC1b humidity controller. Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):629-40. doi:, 10.1107/S2059798316003065. Epub 2016 Apr 26. PMID:27139626 doi:http://dx.doi.org/10.1107/S2059798316003065
