<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Dias, J. M.</style></author><author><style face="normal" font="default" size="100%">Cunha, C. A.</style></author><author><style face="normal" font="default" size="100%">Teixeira, S.</style></author><author><style face="normal" font="default" size="100%">Almeida, G.</style></author><author><style face="normal" font="default" size="100%">Costa, C.</style></author><author><style face="normal" font="default" size="100%">Lampreia, J.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Romao, M. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Crystallization and preliminary X-ray analysis of a membrane-bound nitrite reductase from Desulfovibrio desulfuricans ATCC 27774</style></title><secondary-title><style face="normal" font="default" size="100%">Acta Crystallogr D Biol Crystallogr</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/chemistry/isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallization</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/classification/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophoresis, Polyacrylamide Gel</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins/*chemistry/isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Nitrite Reductases/*chemistry/isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Sodium Dodecyl Sulfate</style></keyword><keyword><style  face="normal" font="default" size="100%">X-ray diffraction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=10666610 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">Pt 2</style></number><volume><style face="normal" font="default" size="100%">56</style></volume><pages><style face="normal" font="default" size="100%">215-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Nitrite reductase from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774 is a multihaem (type c) membrane-bound enzyme that catalyzes the dissimilatory conversion of nitrite to ammonia. Crystals of the oxidized form of this enzyme were obtained using PEG and CaCl(2) as precipitants in the presence of 3--(decylmethylammonium)propane-1-sulfonate and belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 78.94, b = 104.59, c = 143.18 A. A complete data set to 2.30 A resolution was collected using synchrotron radiation at the ESRF. However, the crystals may diffract to beyond 1.7 A and high-resolution data will be collected in the near future.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">10666610</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0907-4449 (Print)0907-4449 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Departamento de Quimica, Centro de Quimica Fina e Biotecnologia, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2825-114 Monte de Caparica, Portugal.</style></auth-address></record></records></xml>