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![[Figure 3]](wa5120fig3mag.jpg)
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Figure 3
Structure of α-DsbA2ΔN. (a) Ribbon representation of α-DsbA2ΔN (chain B from the crystal structure) showing the thioredoxin domain in blue and catalytic cysteine S atoms as yellow spheres. The helical insertion is shown in grey and the N-terminus of the truncated protein is shown in light green. (b) The four molecules in the asymmetric unit. Chain B is oriented in the same way as in (a) and is shown in dark blue. The relative crystallographic temperature factors of the refined coordinates are shown by the backbone thickness (low to high shown as thin to thick) and for chains A, C and D by colour (low to high coloured from blue to red). (c) The active-site cysteines Cys107 and Cys110 of chain B were modelled in a mixed redox state (shown for chain B, with the 2Fo − Fc electron-density map contoured at 1.0σ). |
![[Figure 3]](wa5120fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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