Intermolecular correlations are necessary to explain diffuse scattering from protein crystals

Peck, A.; Poitevin, F.; Lane, T.J.

doi:10.1107/S2052252518001124

Figure 3
Ensemble models inferred from the Bragg data. (a) Multi-conformer modeling of the CypA electron-density map predicts a minor population of alternate conformers (purple) that radiate from the active site. (b) CypA data sets collected at 180 K and below show two loop conformations between residues 79 and 83; the visualized loop conformations are those modeled in the 100 K data set. Above 180 K, the conformation shown in white is not populated. (c) Model of AP assuming that one active site is tungstate-bound (left) while the other is occupied by water molecules that coordinate the active-site metal ions (right). The 0kl plane of the predicted map from each ensemble model is shown on the right, with a different color scale from Fig. 1