2q2l | pdb_00002q2l

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Crystal Structure of Superoxide Dismutase from P. atrosanguina

File:2q2l.jpg


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2q2l, resolution 2.367Å
Sites: AC1, AC2, AC3, AC4 and AC5
Ligands: IOD, ZN
Activity: Superoxide dismutase, with EC number 1.15.1.1
Domains: Cu-Zn_Superoxide_Dismutase
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



Overview

Superoxide 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.

About this Structure

2Q2L is a Protein complex structure of sequences from Potentilla atrosanguinea. Full crystallographic information is available from OCA.

Reference

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

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