title: Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione.
abstract: A monocysteinic mutant of poplar glutaredoxin (C30S) has been overproduced and purified. The protein has been crystallized in complex with glutathione using the hanging-drop vapour-diffusion technique in the presence of PEG 4000 as a precipitating agent. A native data set was collected at 1.55 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 45.7, b = 49.1, c = 104.8 A. Isomorphous crystals of a selenomethionine derivative were grown under the same conditions. Three data sets were collected at 1.73 A using the FIP synchrotron beamline at the ESRF. The positions of the Se atoms were determined and model rebuilding and refinement are in progress.
authors.affiliation: LCM3B, Groupe Biocristallographie, UMR CNRS 7036, UHP-Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lès-Nancy CEDEX, France.
authors.forename: Katia
authors.initials: K
authors.lastname: D'Ambrosio
authors.forename: Brice
authors.initials: B
authors.lastname: Kauffmann
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
authors.forename: Ettore
authors.initials: E
authors.lastname: Benedetti
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Jacquot
authors.forename: André
authors.initials: A
authors.lastname: Aubry
authors.forename: Catherine
authors.initials: C
authors.lastname: Corbier
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D054477:Glutaredoxins; D005978:Glutathione / Q000737:chemistry*; D016297:Mutagenesis, Site-Directed; D010088:Oxidoreductases; D011506:Proteins / Q000737:chemistry*; D012645:Selenomethionine / Q000737:chemistry; D014197:Trees
chemical_list: D054477:Glutaredoxins; D011506:Proteins; D012645:Selenomethionine; D010088:Oxidoreductases; D005978:Glutathione