title: Expression, purification, crystallization and preliminary crystal structure analysis of the Deinococcus radiodurans organic hydroperoxide-resistance protein.
abstract: The organic hydroperoxide-resistance protein (DR1857) from Deinococcus radiodurans has been expressed, purified and crystallized. The crystals are suitable for X-ray analysis, diffract to at least 2.3 A resolution, have unit-cell parameters a = 45.7, b = 59.6, c = 49.7 A, beta = 90.43 degrees and belong to space group P2(1). The calculated Matthews coefficient of 2.1 A(3) Da(-1) coupled with a calculated solvent content of approximately 42% is consistent with the presence of a homodimer in the asymmetric unit. Here, the methods used in the overexpression and purification of the protein are described and details of crystallization conditions and preliminary X-ray diffraction are provided.
authors.affiliation: Macromolecular Crystallography Group, ESRF, BP 220, F-38043 Grenoble CEDEX, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Meunier-Jamin
authors.forename: Ulrike
authors.initials: U
authors.lastname: Kapp
authors.forename: Gordon
authors.initials: G
authors.lastname: Leonard
authors.forename: Seán
authors.initials: S
authors.lastname: McSweeney
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003001:Cloning, Molecular / Q000379:methods; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D034301:Deinococcus / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins