Open AccessBrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative β‐lactamase‐like protein' from Brucella melitensis
Author(s) -
Abendroth Jan,
Sankaran Banumathi,
Edwards Thomas E.,
Gardberg Anna S.,
Dieterich Shellie,
Bhandari Janhavi,
Napuli Alberto J.,
Van Voorhis Wesley C.,
Staker Bart L.,
Myler Peter J.,
Stewart Lance J.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111010220
Subject(s) - brucella melitensis , phaser , crystallography , chemistry , resolution (logic) , ligand (biochemistry) , crystal (programming language) , crystal structure , physics , biology , optics , brucella , biochemistry , computer science , receptor , virology , artificial intelligence , brucellosis , programming language
The crystal structure of a β‐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.