Crystallization and preliminary X-ray analysis of the tungsten-dependent acetylene hydratase from Pelobacter acetylenicus.
Acetylene hydratase is a tungsten-containing hydroxylase that converts acetylene to acetaldehyde in a unique reaction that requires a strong reductant. The subsequent disproportionation of acetaldehyde yields acetate and ethanol. Crystals of the tungsten/iron-sulfur protein acetylene hydratase from Pelobacter acetylenicus strain WoAcy 1 (DSM 3246) were grown by the vapour-diffusion method in an N2/H2 atmosphere using polyethylene glycol as precipitant. Growth of crystals suitable for X-ray analysis strictly depended on the presence of Ti(III) citrate or dithionite as reducing agents.
Einsle
Oliver
O
Abteilung Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany. oeinsle@gwdg.de
Niessen
Holger
H
Abt
Dietmar J
DJ
Seiffert
Grazyna
G
Schink
Bernhard
B
Huber
Robert
R
Messerschmidt
Albrecht
A
Kroneck
Peter M H
PM
D000595:Amino Acid Sequence; D000693:Anaerobiosis; D001426:Bacterial Proteins / Q000737:chemistry / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D020564:Deltaproteobacteria / Q000201:enzymology*; D006836:Hydro-Lyases / Q000737:chemistry / Q000187:drug effects / Q000302:isolation & purification / Q000378:metabolism*; D012984:Software; D017356:Synchrotrons; D014414:Tungsten / Q000494:pharmacology*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D006836:Hydro-Lyases; C096200:acetylene hydratase; D014414:Tungsten