{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T10:59:29Z","timestamp":1761994769017,"version":"build-2065373602"},"reference-count":43,"publisher":"International Union of Crystallography (IUCr)","issue":"12","license":[{"start":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T00:00:00Z","timestamp":1480032000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T00:00:00Z","timestamp":1480032000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"published-print":{"date-parts":[[2016,12,1]]},"abstract":"<jats:p>In bacteria, the second committed step in the diaminopimelate\/lysine anabolic pathways is catalyzed by the enzyme dihydrodipicolinate reductase (DapB). DapB catalyzes the reduction of dihydrodipicolinate to yield tetrahydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of DapB from the human-pathogenic bacterium<jats:italic>Bartonella henselae<\/jats:italic>, the causative bacterium of cat-scratch disease, are reported. Protein crystals were grown in conditions consisting of 5%(<jats:italic>w<\/jats:italic>\/<jats:italic>v<\/jats:italic>) PEG 4000, 200\u2005m<jats:italic>M<\/jats:italic>sodium acetate, 100\u2005m<jats:italic>M<\/jats:italic>sodium citrate tribasic pH 5.5 and were shown to diffract to \u223c2.3\u2005\u00c5 resolution. They belonged to space group<jats:italic>P<\/jats:italic>4<jats:sub>3<\/jats:sub>22, with unit-cell parameters<jats:italic>a<\/jats:italic>= 109.38,<jats:italic>b<\/jats:italic>= 109.38,<jats:italic>c<\/jats:italic>= 176.95\u2005\u00c5.<jats:italic>R<\/jats:italic><jats:sub>r.i.m.<\/jats:sub>was 0.11,<jats:italic>R<\/jats:italic><jats:sub>work<\/jats:sub>was 0.177 and<jats:italic>R<\/jats:italic><jats:sub>free<\/jats:sub>was 0.208. The three-dimensional structural features of the enzymes show that DapB from<jats:italic>B. henselae<\/jats:italic>is a tetramer consisting of four identical polypeptides. In addition, the substrate NADP<jats:sup>+<\/jats:sup>was found to be bound to one monomer, which resulted in a closed conformational change in the N-terminal domain.<\/jats:p>","DOI":"10.1107\/s2053230x16018525","type":"journal-article","created":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T16:23:20Z","timestamp":1480091000000},"page":"885-891","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":2,"title":["The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium<i>Bartonella henselae<\/i>strain Houston-1 at 2.3\u2005\u00c5 resolution"],"prefix":"10.1107","volume":"72","author":[{"given":"Ali R.","family":"Cala","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria T.","family":"Nadeau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Abendroth","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bart L.","family":"Staker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexandra R.","family":"Reers","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anthony W.","family":"Weatherhead","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renwick C. 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