Open AccessCrystallization and preliminary X‐ray diffraction analysis of the complex between a human anti‐alpha toxin antibody fragment and alpha toxin
Author(s) -
Oganesyan Vaheh,
Barnes Arnita,
Tkaczyk Christine,
Ferguson Andrew,
Wu Herren,
Dall'Acqua William F.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113002881
Subject(s) - monoclinic crystal system , crystallization , toxin , crystallography , antibody , chemistry , monomer , alpha (finance) , stereochemistry , crystal structure , biology , biochemistry , medicine , immunology , polymer , construct validity , nursing , organic chemistry , patient satisfaction
Staphylococcus aureus alpha toxin (AT) has been crystallized in complex with the Fab fragment of a human antibody (MEDI4893). This constitutes the first reported crystals of AT bound to an antibody. The monoclinic crystals belonged to space group P 2 1 , with unit‐cell parameters a = 85.52, b = 148.50, c = 93.82 Å, β = 99.82°. The diffraction of the crystals extended to 2.56 Å resolution. The asymmetric unit contained two MEDI4893 Fab–AT complexes. This corresponds to a crystal volume per protein weight ( V M ) of 2.3 Å 3 Da −1 and a solvent content of 47%. The three‐dimensional structure of this complex will contribute to an understanding of the molecular basis of the interaction of MEDI4893 with AT. It will also shed light on the mechanism of action of this antibody, the current evaluation of which in the field of S. aureus ‐mediated diseases makes it a particularly interesting case study. Finally, this study will provide the three‐dimensional structure of AT in a monomeric state for the first time.