Crystallization and preliminary crystallographic analysis of Rieske iron-sulfur protein II (soxF) from sulfolobus acidocaldarius.
An archaeal Rieske iron-sulfur protein has been crystallized for the first time. The genetically constructed soluble form of the soxF protein was expressed in E. coli. It contains a correctly inserted [2Fe--2S] cluster. The authentic soxF protein is part of a terminal oxidase complex in the respiratory chain of the hyperthermoacidophilic crenarchaeon Sulfolobus acidocaldarius (DSM 639). The enzyme crystallizes in the space group P6(1) or P6(5), with unit-cell parameters a = b = 80.19, c = 75.69 A. A complete data set has been collected to 1.64 A resolution at 100 K.
Bönisch
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Karolinska Institutet, Department of Bioscience at NOVUM, Centre for Structural Biochemistry, Hälsovägen 7, S-14157 Huddinge, Sweden.
Schmidt
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CL
Schäfer
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Ladenstein
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R
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D014450:Electron Transport Complex III; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D012984:Software; D016945:Sulfolobus acidocaldarius / Q000378:metabolism*
D007506:Iron-Sulfur Proteins; D011994:Recombinant Proteins; C037989:Rieske iron-sulfur protein; D014450:Electron Transport Complex III