A His-tagged derivative of the multidrug efflux pump AcrB could be crystallized in three different space groups (R3, R32 and P321). Experimental MAD-phasing maps from R32 AcrBHis crystals were obtained to a resolution of 3.5 Å. Datasets of native and substrate soaked AcrB His crystals were collected at the Swiss Light Source X06SA beamline up to a resolution of 2.7 Å and refinement of these data provided good quality electron density maps, which allowed us to complement the published AcrB structure (PDB code 1iwg). Introduction of amino acids 860-865 and 868 lacking in the 1iwg structure and deletion of a highly disordered region (amino acids 669-678) improved Rfree and average B factors in the 2.7 Å model. We could not identify significant densities indicating specific antibiotic binding sites in the AcrB R32 space group datasets under the soaking conditions tested. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
Pos, K. M., Schiefner, A., Seeger, M. A., & Diederichs, K. (2004). Crystallographic analysis of AcrB. In FEBS Letters (Vol. 564, pp. 333–339). https://doi.org/10.1016/S0014-5793(04)00272-8