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Figure 3
Structure of VapD. (a) Approximately orthogonal views of the VapD chain represented as a ribbon trace and colour-ramped from the N-terminus (blue) to the C-terminus (red). The secondary-structure elements are labelled. (b) Stereoview of the electron density (2FoFc) contoured at the 1σ level and displayed on the side-chain amide-containing residues, which form a closed hydrogen-bonding network on the surface of VapD. (c) Electrostatic surface rendering of VapD with positive electrostatic potential in blue and negative electrostatic potential in red. The extended apolar surfaces are evident. The orientation of the molecule in each case is apparent from the adjacent ribbon rendering. (d) The C-terminal residues of VapD: the chain is shown as a cyan ribbon with residues 124–134 in cylinder format coloured by atom and labelled. These and subsequent structural figures were produced using CCP4mg (McNicholas et al., 2011BB26).

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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