@article {2339,
	title = {Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16: purification, crystallization and preliminary X-ray analysis},
	journal = {Acta Crystallogr Sect F Struct Biol Cryst Commun},
	volume = {63},
	number = {Pt 6},
	year = {2007},
	note = {<p>1744-3091 (Electronic)1744-3091 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Jun 1},
	pages = {516-9},
	abstract = {<p>The periplasmic nitrate reductase from Cupriavidus necator (also known as Ralstonia eutropha) is a heterodimer that is able to reduce nitrate to nitrite. It comprises a 91 kDa catalytic subunit (NapA) and a 17 kDa subunit (NapB) that is involved in electron transfer. The larger subunit contains a molybdenum active site with a bis-molybdopterin guanine dinucleotide cofactor as well as one [4Fe-4S] cluster, while the small subunit is a di-haem c-type cytochrome. Crystals of the oxidized form of this enzyme were obtained using polyethylene glycol 3350 as precipitant. A single crystal grown at the High Throughput Crystallization Laboratory of the EMBL in Grenoble diffracted to beyond 1.5 A at the ESRF (ID14-1), which is the highest resolution reported to date for a nitrate reductase. The unit-cell parameters are a = 142.2, b = 82.4, c = 96.8 A, beta = 100.7 degrees, space group C2, and one heterodimer is present per asymmetric unit.</p>
},
	keywords = {Bacterial Proteins/chemistry/*isolation \& purification, Crystallization/methods, Crystallography, X-Ray, Cupriavidus necator/*isolation \& purification, Dimerization, Nitrate Reductase/chemistry/*isolation \& purification, Protein Subunits/chemistry/isolation \& purification},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=17554176 },
	author = {Coelho, C. and Gonzalez, P. J. and Trincao, J. and Carvalho, A. L. and Najmudin, S. and Hettman, T. and Dieckman, S. and Moura, J. J. and Moura, I. and Romao, M. J.}
}
