Structure of the virulence-associated protein VapD from the intracellular pathogen Rhodococcus equi

Whittingham, J.L.; Blagova, E.V.; Finn, C.E.; Luo, H.; Miranda-CasoLuengo, R.; Turkenburg, J.P.; Leech, A.P.; Walton, P.H.; Murzin, A.G.; Meijer, W.G.; Wilkinson, A.J.

doi:10.1107/S1399004714012632

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 2
Physical properties of purified Vap proteins. (a) 15% SDS–PAGE analysis (molecular-weight markers 66.2, 31.0, 21.5 and 14.4 kDa) showing the effects of chymotrypsin digestion on VapD-full at a chymotrypsin:VapD weight ratio of 1:100. Lanes 1 and 2 are from the same gel, although intervening lanes have been cropped. (b) Circular-dichroism spectra of VapD-full and VapD-core. (c) SEC-MALLS analyses of VapD-full and VapD-core. The refractive index (RI) of the eluate from the Superdex S75 column is plotted as a function of time. For the principal peaks, the molecular weight (MW) of the species in the eluate is calculated from light-scattering measurements.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 8| July 2014| Pages 2139-2151

doi:10.1107/S1399004714012632

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