2Q2L

Crystal Structure of Superoxide Dismutase from P. atrosanguina

Summary for 2Q2L

• Entry DOI: 10.2210/pdb2q2l/pdb
• Descriptor: Superoxide Dismutase, ZINC ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: sod; sad; antioxidant; oxidoreductase; metal-binding, oxidoreductase
• Biological source: Potentilla atrosanguinea
• Total number of polymer chains: 2
• Total formula weight: 31831.60

Authors

Manickam, Y.,Gill, J.,Mishra, P.C.,Sharma, A. (deposition date: 2007-05-29, release date: 2008-03-25, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.367 Å)