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

Abendroth, J.; Sankaran, B.; Edwards, T.E.; Gardberg, A.S.; Dieterich, S.; Bhandari, J.; Napuli, A.J.; Van Voorhis, W.C.; Staker, B.L.; Myler, P.J.; Stewart, L.J.

doi:10.1107/S1744309111010220

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Dinuclear manganese center. The active site of BrabA.11339.a consists of two manganese ions (magenta), which are bridged by a water molecule (red). The phosphate group of GMP is in close proximity to this activated water molecule. The σ_A-weighted 2F_o − F_c electron density for the high-resolution data set is contoured at 1σ (blue) and the corresponding F_o − F_c electron density is contoured at ±3σ (green/red). The anomalous Fourier electron density is contoured at 10σ (orange). The strong anomalous Fourier density at all three wavelengths indentifies the active-site metal as manganese. For bond distances refer to Table 3

; for anomalous peak heights refer to Table 4

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 67| Part 9| August 2011| Pages 1106-1112

doi:10.1107/S1744309111010220

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