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![[Figure 3]](qq5002fig3mag.jpg)
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Figure 3
(a) Examples of (i) disulfide-bond cleavage, (ii) glutamate decarboxylation and (iii) methionine methylthio group disordering in an Fobs(late) − Fobs(early) difference map calculated for a structure of Torpedo californica acetylcholinesterase (PDB entry 1qid; Weik et al., 2000  ). The maps are contoured at ±4σ, with positive and negative difference density coloured green and red, respectively. This figure was adapted from Bury, Carmichael et al. (2016). (b) A disulfide bond modelled in both oxidized and reduced conformations to account for radiation damage in a structure of the tumour necrosis factor protein BAFF bound to a bhpBR3 peptide (PDB entry 3v56; Smart et al., 2012). The oxidized and reduced conformers of the cysteine side chain that undergoes a large conformational change are indicated with arrows. The 2mFobs − DFcalc map (blue) is contoured at 1.5 r.m.s.d.; the Fobs − Fcalc difference density map is contoured at ± 3.0 r.m.s.d., with positive and negative density coloured green and red, respectively. (c) A representation of the specific damage suffered by low-dose and high-dose data sets collected for the C.Esp1396 protein in complex with its target DNA sequence. Damage artefacts are represented as spheres: the spheres are coloured blue and red depending on whether they are within 2 Å of or further than 2 Å from the DNA, respectively. The radius of each sphere is proportional to the electron-density loss (electrons per Å3). This figure was adapted from Bury et al. (2015). All data leading to these structures were collected at 100 K. |
![[Figure 3]](qq5002fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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