title: Crystallization and preliminary diffraction studies of native and selenomethionine CcmG (CycY, DsbE).
abstract: Disulfide-bond (Dsb) proteins are a family of redox proteins containing a Cys-X-X-Cys motif. They are essential for disulfide-bond exchange in the bacterial periplasm and are necessary for the correct folding and function of many secreted proteins. CcmG (DsbE) is a reducing Dsb protein required for cytochrome c maturation. Crystals of Bradyrhizobium japonicum CcmG have been obtained that diffract X-rays to 1.14 A resolution. The crystals are orthorhombic, space group P2(1)2(1)2(1), with unit-cell parameters a = 35.1, b = 48.2, c = 90.2 A. Selenomethionine CcmG was expressed without using a methionine auxotroph or methionine-pathway inhibition and was purified without reducing agents.
authors.affiliation: Centre for Drug Design and Development and Special Research Centre for Functional and Applied Genomics, Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD 4072, Australia.
authors.forename: M A
authors.initials: MA
authors.lastname: Edeling
authors.forename: L W
authors.initials: LW
authors.lastname: Guddat
authors.forename: R A
authors.initials: RA
authors.lastname: Fabianek
authors.forename: J A
authors.initials: JA
authors.lastname: Halliday
authors.forename: A
authors.initials: A
authors.lastname: Jones
authors.forename: L
authors.initials: L
authors.lastname: Thöny-Meyer
authors.forename: J L
authors.initials: JL
authors.lastname: Martin
mesh_terms: D019943:Amino Acid Substitution; D020369:Bradyrhizobium / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D033903:Periplasmic Proteins; D011487:Protein Conformation; D012645:Selenomethionine / Q000737:chemistry*
chemical_list: D033903:Periplasmic Proteins; D012645:Selenomethionine; D010088:Oxidoreductases; C077913:periplasmic protein disulfide oxidoreductase