The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.

Lund BA, Thomassen AM, Nesheim BHB, Carlsen TJO, Isaksson J, Christopeit T, Leiros HS
FEBS J (2018 Aug 28)
PMID: 30153368
doi: 10.1111/febs.14643 		Submitted to SASBDB: 2018 Aug 30
Published in SASBDB:

SASDEM3 – Dimeric class D beta-lactamase OXA-48

Beta-lactamase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-lactamase dimer, 56 kDa Klebsiella pneumoniae protein
Buffer: 50 mM HEPES 50 mM K2SO4, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 23
RgGuinier 2.5 nm
Dmax 7.4 nm
VolumePorod 74 nm3