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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2015,4,7]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Racemic protein crystallography was used to determine the X-ray structure of the predicted\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    protein Rv1738, which had been completely recalcitrant to crystallization in its natural\n                    <jats:sc>l<\/jats:sc>\n                    -form. Native chemical ligation was used to synthesize both\n                    <jats:sc>l<\/jats:sc>\n                    -protein and\n                    <jats:sc>d<\/jats:sc>\n                    -protein enantiomers of Rv1738. Crystallization of the racemic {\n                    <jats:sc>d<\/jats:sc>\n                    -protein +\n                    <jats:sc>l<\/jats:sc>\n                    -protein} mixture was immediately successful. The resulting crystals diffracted to high resolution and also enabled facile structure determination because of the quantized phases of the data from centrosymmetric crystals. The X-ray structure of Rv1738 revealed striking similarity with bacterial hibernation factors, despite minimal sequence similarity. We predict that Rv1738, which is highly up-regulated in conditions that mimic the onset of persistence, helps trigger dormancy by association with the bacterial ribosome.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1422387112","type":"journal-article","created":{"date-parts":[[2015,3,23]],"date-time":"2015-03-23T23:17:43Z","timestamp":1427152663000},"page":"4310-4315","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":46,"title":["A functional role of Rv1738 in\n                    <i>Mycobacterium tuberculosis<\/i>\n                    persistence suggested by racemic protein crystallography"],"prefix":"10.1073","volume":"112","author":[{"given":"Richard D.","family":"Bunker","sequence":"first","affiliation":[{"name":"Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1142, New Zealand; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kalyaneswar","family":"Mandal","sequence":"additional","affiliation":[{"name":"Department of Chemistry,"},{"name":"Department of Biochemistry and Molecular Biology, and"},{"name":"Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ghader","family":"Bashiri","sequence":"additional","affiliation":[{"name":"Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1142, New Zealand; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica J.","family":"Chaston","sequence":"additional","affiliation":[{"name":"Maurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, Auckland 1142, New Zealand; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bradley L.","family":"Pentelute","sequence":"additional","affiliation":[{"name":"Department of Chemistry,"},{"name":"Department of Biochemistry and Molecular Biology, and"},{"name":"Institute for Biophysical Dynamics, University of Chicago, Chicago, IL 60637"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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