Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione(1135 views) D'Ambrosio K, Kauffmann B, Rouhier N, Benedetti E, Jacquot JP, Aubry A, Corbier C
Keywords: Glutaredoxin, Glutathione, Oxidoreductase, Protein, Selenomethionine, Article, Chemistry, Crystallization, Molecular Cloning, Polyacrylamide Gel Electrophoresis, Site Directed Mutagenesis, X Ray Crystallography, X-Ray, Site-Directed, Trees, Populus Berolinensis,
Affiliations: *** IBB - CNR ***
LCM3B, Groupe Biocristallographie, Faculté des Sciences, BP 239, 54506 Vandoeuvre-les-Nancy CEDEX, France
Ist. di Biostrutture e Bioimmagini, CNR, Univ. Studi di Napoli Federico II, 80134 Napoli, Italy
Intrac. Arbres M., UHP-Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-les-Nancy CEDEX, France
References: Not available.
Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione
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 Angstrom 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 Angstrom. Isomorphous crystals of a selenomethionine derivative were grown under the same conditions. Three data sets were collected at 1.73 Angstrom using the FIP synchrotron beamline at the ESRF. The positions of the Se atoms were determined and model rebuilding and refinement are in progress.
Crystallization and preliminary X-ray studies of the glutaredoxin from poplar in complex with glutathione