BrabA.11339.a: Anomalous diffraction and ligand binding guide towards the elucidation of the function of a putative Β-lactamase-like protein from Brucella melitensis

4Citations
Citations of this article
20Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

Abendroth, J., Sankaran, B., Edwards, T. E., Gardberg, A. S., Dieterich, S., Bhandari, J., … Stewart, L. J. (2011). BrabA.11339.a: Anomalous diffraction and ligand binding guide towards the elucidation of the function of a putative Β-lactamase-like protein from Brucella melitensis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(9), 1106–1112. https://doi.org/10.1107/S1744309111010220

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free