Fig. 1: A 3.9 Å D8 symmetry averaged cryoEM structure of MmCpn in the presence of ATP. | Nature Communications

Fig. 1: A 3.9 Å D8 symmetry averaged cryoEM structure of MmCpn in the presence of ATP.

From: CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin

Fig. 1

a Top and side views of MmCpn cryoEM reconstruction. b Local resolution map calculated by MonoRes51. Color key for local resolution (in Å) is shown. c Segmented cryoEM map for a single subunit with the model superimposed. Equatorial, intermediate, and apical domains of the model are colored in green, yellow, and red respectively. High-resolution features in the equatorial domain are shown in side panels, including the ATP binding site (upper right with an arrow).

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