{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,1]],"date-time":"2025-11-01T09:34:55Z","timestamp":1761989695220,"version":"build-2065373602"},"reference-count":40,"publisher":"International Union of Crystallography (IUCr)","issue":"1","license":[{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"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":[[2016,1,1]]},"abstract":"<jats:p>The enzyme dihydrodipicolinate synthase catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis. Dihydrodipicolinate synthase catalyzes the condensation of L-aspartate 4-semialdehyde and pyruvate to synthesize L-2,3-dihydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the pathogenic bacterium<jats:italic>Bartonella henselae<\/jats:italic>, the causative bacterium of cat-scratch disease, are presented. Protein crystals were grown in conditions consisting of 20%(<jats:italic>w<\/jats:italic>\/<jats:italic>v<\/jats:italic>) PEG 4000, 100\u2005m<jats:italic>M<\/jats:italic>sodium citrate tribasic pH 5.5 and were shown to diffract to \u223c2.10\u2005\u00c5 resolution. They belonged to space group<jats:italic>P<\/jats:italic>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>2<jats:sub>1<\/jats:sub>, with unit-cell parameters<jats:italic>a<\/jats:italic>= 79.96,<jats:italic>b<\/jats:italic>= 106.33,<jats:italic>c<\/jats:italic>= 136.25\u2005\u00c5. The final<jats:italic>R<\/jats:italic>values were<jats:italic>R<\/jats:italic><jats:sub>r.i.m.<\/jats:sub>= 0.098,<jats:italic>R<\/jats:italic><jats:sub>work<\/jats:sub>= 0.183,<jats:italic>R<\/jats:italic><jats:sub>free<\/jats:sub>= 0.233.<\/jats:p>","DOI":"10.1107\/s2053230x15023213","type":"journal-article","created":{"date-parts":[[2015,12,13]],"date-time":"2015-12-13T05:41:00Z","timestamp":1449985260000},"page":"2-9","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":5,"title":["Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium<i>Bartonella henselae<\/i>strain Houston-1 at 2.1\u2005\u00c5 resolution"],"prefix":"10.1107","volume":"72","author":[{"given":"Kubra F.","family":"Naqvi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bart L.","family":"Staker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renwick C. 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