Open AccessCrystallization and preliminary X‐ray analysis of a novel dye‐linked l ‐proline dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix
Author(s) -
Satomura Takenori,
Sakuraba Haruhiko,
Hara Yusuke,
Ohshima Toshihisa
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110036808
Subject(s) - tetragonal crystal system , crystallization , crystallography , polyethylene glycol , solvent , proline , chemistry , dehydrogenase , materials science , nuclear chemistry , crystal structure , enzyme , amino acid , biochemistry , organic chemistry
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 P 4 1 2 1 2 or its enantiomorph P 4 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 K α 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%.