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- W2004605701 abstract "Significance Racemic protein crystallography was used to determine the X-ray structure of the predicted Mycobacterium tuberculosis protein Rv1738, which had been completely recalcitrant to crystallization in its natural l -form. Native chemical ligation was used to synthesize both l -protein and d -protein enantiomers of Rv1738. Crystallization of the racemic { d -protein + l -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." @default.
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- W2004605701 date "2015-03-23" @default.
- W2004605701 modified "2023-10-12" @default.
- W2004605701 title "A functional role of Rv1738 in <i>Mycobacterium tuberculosis</i> persistence suggested by racemic protein crystallography" @default.
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- W2004605701 doi "https://doi.org/10.1073/pnas.1422387112" @default.
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