Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

Nogly, P.; James, D.; Wang, D.; White, T.A.; Zatsepin, N.; Shilova, A.; Nelson, G.; Liu, H.; Johansson, L.; Heymann, M.; Jaeger, K.; Metz, M.; Wickstrand, C.; Wu, W.; Båth, P.; Berntsen, P.; Oberthuer, D.; Panneels, V.; Cherezov, V.; Chapman, H.; Schertler, G.; Neutze, R.; Spence, J.; Moraes, I.; Burghammer, M.; Standfuss, J.; Weierstall, U.

doi:10.1107/S2052252514026487

Figure 3
(Centre) Comparison of bR structures solved by SMX and conventional cryocrystallography (Cryo). The protein backbone of the room-temperature SMX structure (purple) superimposes well with the Cryo structure (blue). (Bottom) Retinal omit maps [blue (Cryo) or purple (SMX) mesh, 2F_o − F_c at 1.5σ; green mesh, F_o − F_c at 2.5σ] indicate increased flexibility in the β-ionone ring. The upper insets show a different rotamer for E194 involved in proton translocation, and indications for radiation damage on D38 exposed to the extramembrane environment.

IUCrJ

Volume 2| Part 2| January 2015| Pages 168-176

ISSN: 2052-2525

doi:10.1107/S2052252514026487

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