2Q2L

Crystal Structure of Superoxide Dismutase from P. atrosanguina

2Q2L の概要

• エントリーDOI: 10.2210/pdb2q2l/pdb
• 分子名称: Superoxide Dismutase, ZINC ION, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: sod; sad; antioxidant; oxidoreductase; metal-binding, oxidoreductase
• 由来する生物種: Potentilla atrosanguinea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31831.60

構造登録者

Manickam, Y.,Gill, J.,Mishra, P.C.,Sharma, A. (登録日: 2007-05-29, 公開日: 2008-03-25, 最終更新日: 2024-10-30)

主引用文献

Yogavel, M.,Gill, J.,Mishra, P.C.,Sharma, A.
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
Acta Crystallogr.,Sect.D, 63:931-934, 2007

PubMed Abstract: 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.

PubMed: 17642520
DOI: 10.1107/S0907444907029174

実験手法

X-RAY DIFFRACTION (2.367 Å)