Structure fluctuations of proteins crystallized in different space groups.

<p>Structures in different crystal forms serve as a control for the expected structural flexibility. (a) We compared the distribution of minGDTs depending on the number of crystal forms (space groups). (b) The average minGDTs are displayed for the proteins of three space groups (‘SP’, red), time-averaged refinements (cyan), and NMR ensembles (purple). The minGDTs of the latter two (cyan and purple) were computed from resampled ensembles of three random structures. Generated ensembles approached the structural variability seen between different space groups of the same protein at pTLS = 1.