Crystallization and preliminary crystallographic analysis of the high-potential iron-sulfur protein from Thermochromatium tepidum.
The high-potential iron-sulfur protein (HiPIP) is an electron carrier between the photosynthetic reaction centre and the cytochrome bc(1) complex in the electron-transfer chain of photosynthesis. The purified HiPIP from Thermochromatium tepidum (formerly Chromatium tepidum) was crystallized in a solution of 1.4 M ammonium sulfate and 0.1 M sodium citrate pH 3.5. The crystals diffract X-rays beyond 1.4 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.12 (6), b = 59.59 (10), c = 23.62 (3) A. The structure was preliminarily solved by the molecular-replacement method. The crystal structure of HiPIP from T. tepidum showed that the proteins exist as monomers, although HiPIPs from several other species can form dimers.
Nogi
T
T
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606--8502, Japan.
Kobayashi
M
M
Nozawa
T
T
Miki
K
K
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D002844:Chromatium / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D019281:Dimerization; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000302:isolation & purification; D045322:Photosynthetic Reaction Center Complex Proteins
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein