title: Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum.
abstract: Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) > 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Japan.
authors.forename: Lijun
authors.initials: L
authors.lastname: Liu
authors.forename: Terukazu
authors.initials: T
authors.lastname: Nogi
authors.forename: Masayuki
authors.initials: M
authors.lastname: Kobayashi
authors.forename: Tsunenori
authors.initials: T
authors.lastname: Nozawa
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002841:Chromatiaceae / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods*; D004583:Electrons; D006860:Hydrogen Bonding; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular; D013696:Temperature
chemical_list: D007506:Iron-Sulfur Proteins