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This work reports the crystal structure of BsrV, the broad spectrum racemase of Vibrio cholerae (1.15 Å resolution); unveils signature amino acids associated to its multispecificity and uses this signature sequence to identify a large family of BsrV-like multi-specific racemases in bacteria. Structural analyses of an additional Bsr confirmed the distinguishing features are conserved among Bsr-family members.

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A set of seven caged gadolinium complexes were shown to be excellent compounds for introducing anomalous scatterers into protein crystals for de novo anomalous phasing. Their high phasing power and versatile binding modes make them highly suitable as a heavy-atom screen.
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