@article {2540,
	title = {Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers},
	journal = {Eur J Biochem},
	volume = {215},
	number = {3},
	year = {1993},
	note = {<p>0014-2956 (Print)0014-2956 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Aug 1},
	pages = {729-32},
	abstract = {<p>The Desulfovibrio gigas aldehyde oxidoreductase contains molybdenum bound to a pterin cofactor and [2Fe-2S] centers. The enzyme was characterized by SDS/PAGE, gel-filtration and analytical ultracentrifugation experiments. It was crystallized at 4 degrees C, pH 7.2, using isopropanol and MgCl2 as precipitants. The crystals diffract beyond 0.3-nm (3.0-A) resolution and belong to space group P6(1)22 or its enantiomorph, with cell dimensions a = b = 14.45 nm and c = 16.32 nm. There is one subunit/asymmetric unit which gives a packing density of 2.5 x 10(-3) nm3/Da (2.5 A3/Da), consistent with the experimental crystal density, rho = 1.14 g/cm3. One dimer (approximately 2 x 100 kDa) is located on a crystallographic twofold axis.</p>
},
	keywords = {Aldehyde Oxidoreductases/*chemistry, Amino Acid Sequence, Crystallization, Desulfovibrio/*enzymology, Iron-Sulfur Proteins/*analysis, Molecular Sequence Data, Molecular Weight, Molybdenum/*analysis, X-ray diffraction},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=8354279 },
	author = {Romao, M. J. and Barata, B. A. and Archer, M. and Lobeck, K. and Moura, I. and Carrondo, M. A. and Legall, J. and Lottspeich, F. and Huber, R. and Moura, J. J.}
}
