Crystallization and preliminary X-ray analysis of a novel dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix.
A novel dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix was crystallized using the sitting-drop vapour-diffusion method with polyethylene glycol 8000 as the precipitant. The crystals belonged to the tetragonal space group P4(1)2(1)2 or its enantiomorph P4(3)2(1)2, with unit-cell parameters a = b = 61.1, c = 276.3 Å, and diffracted to 2.87 Å resolution using a Cu Kα rotating-anode generator with an R-AXIS VII detector. The asymmetric unit contained one protein molecule, giving a crystal volume per enzyme mass (V(M)) of 2.75 Å(3) Da(-1) and a solvent content of 55.3%.
Department of Materials Science, Yonago National College of Technology, 4448 Hikona-cho, Yonago, Tottori 683-8506, Japan.
Takenori
T
Satomura
Haruhiko
H
Sakuraba
Yusuke
Y
Hara
Toshihisa
T
Ohshima
D041522:Aeropyrum / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011394:Proline Oxidase / Q000737:chemistry*
D011394:Proline Oxidase