@article {2457,
	title = {Crystallization and preliminary x-ray analysis of a nitrate reductase from Desulfovibrio desulfuricans ATCC 27774},
	journal = {Acta Crystallogr D Biol Crystallogr},
	volume = {55},
	number = {Pt 4},
	year = {1999},
	note = {<p>0907-4449 (Print)0907-4449 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Apr},
	pages = {877-9},
	abstract = {<p>Periplasmic nitrate reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 contains two molybdopterin guanine dinucleotide cofactors and one [4Fe-4S] cluster as prosthetic groups and catalyzes the conversion of nitrate to nitrite. Crystals of the oxidized form of this enzyme were obtained using PEG as precipitant and belong to space group P3121 or P3221, with unit-cell dimensions a = b = 106.3, c = 135.1 A. There is one monomer of 80 kDa in the asymmetric unit, which corresponds to a Matthews ratio of 2.75 A3 Da-1. Using cryo-cooling procedures and X-rays from a rotating-anode generator, diffraction was observed to beyond 3.0 A resolution.</p>
},
	keywords = {Bacterial Proteins/*chemistry/isolation \& purification, Crystallization, Crystallography, X-Ray, Desulfovibrio/*enzymology, Nitrate Reductase, Nitrate Reductases/*chemistry/isolation \& purification},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=10089321 },
	author = {Dias, J. M. and Bursakov, S. and Carneiro, C. and Moura, J. J. and Moura, I. and Romao, M. J.}
}
