3py5

Publication Abstract from PubMed

The crystal structure of a beta-lactamase-like protein from Brucella melitensis was initially solved by SAD phasing from an in-house data set collected on a crystal soaked with iodide. A high-resolution data set was collected at a synchroton at the Se edge wavelength, which also provided an independent source of phasing using a small anomalous signal from metal ions in the active site. Comparisons of anomalous peak heights at various wavelengths allowed the identification of the active-site metal ions as manganese. In the native data set a partially occupied GMP could be identified. When co-crystallized with AMPPNP or GMPPNP, clear density for the hydrolyzed analogs was observed, providing hints to the function of the protein.

BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative beta-lactamase-like protein' from Brucella melitensis.,Abendroth J, Sankaran B, Edwards TE, Gardberg AS, Dieterich S, Bhandari J, Napuli AJ, Van Voorhis WC, Staker BL, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1106-12. Epub 2011 Aug 16. PMID:21904058^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.