2q2l
From Proteopedia
Crystal Structure of Superoxide Dismutase from P. atrosanguina
Structural highlights
FunctionB2CP37_9ROSA Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000393] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSuperoxide dismutase (SOD) from Potentilla atrosanguinea (Wall. ex. Lehm.) was crystallized using 20% PEG 3350 and 0.2 M ammonium iodide and diffraction data were collected to 2.36 A resolution using an in-house Cu Kalpha X-ray source. Analyses show that data with a redundancy of 3.2 were sufficient to determine the structure by the SAD technique using the iodine anomalous signal. This redundancy is lower than that in previous cases in which protein structures were determined using iodines for phasing and in-house copper X-ray sources. Cocrystallization of proteins with halide salts such as ammonium iodide in combination with copper-anode X-ray radiation can therefore serve as a powerful and easy avenue for structure solution. SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution.,Yogavel M, Gill J, Mishra PC, Sharma A Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):931-4. Epub 2007, Jul 17. PMID:17642520[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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