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 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.
D'Ambrosio
Katia
K
LCM3B, Groupe Biocristallographie, UMR CNRS 7036, UHP-Nancy 1, Faculté des Sciences, BP 239, 54506 Vandoeuvre-lès-Nancy CEDEX, France.
Kauffmann
Brice
B
Rouhier
Nicolas
N
Benedetti
Ettore
E
Jacquot
Jean-Pierre
JP
Aubry
André
A
Corbier
Catherine
C
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
D054477:Glutaredoxins; D011506:Proteins; D012645:Selenomethionine; D010088:Oxidoreductases; D005978:Glutathione