Neutron scattering in the biological sciences: progress and prospects

Ashkar, R.; Bilheux, H.; Bordallo, H.; Briber, R.; Callaway, D.J.E.; Cheng, X.; Chu, X.-Q.; Curtis, J.E.; Dadmun, M.; Fenimore, P.; Fushman, D.; Gabel, F.; Gupta, K.; Herberle, F.; Heinrich, F.; Hong, L.; Katsaras, J.; Kelman, Z.; Kharlampieva, E.; Kneller, G.R.; Kovalevsky, A.; Krueger, S.; Langan, P.; Lieberman, R.; Liu, Y.; Losche, M.; Lyman, E.; Mao, Y.; Marino, J.; Mattos, C.; Meilleur, F.; Moody, P.; Nickels, J.D.; O'Dell, W.B.; O'Neill, H.; Perez-Salas, U.; Peters, J.; Petridis, L.; Sokolov, A.P.; Stanley, C.; Wagner, N.; Weinrich, M.; Weiss, K.; Wymore, T.; Zhang, Y.; Smith, J.C.

doi:10.1107/S2059798318017503

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 11
Determination of membrane-protein structures using NR. (a) Proteins embedded in a substrate-supported, in-plane fluid bilayer (lower left) are measured at various solvent contrasts. (b) Integrative modeling uses diverse sources of information, such as protein crystal structures, to model the NR data using rigid-body placement algorithms that determine the penetration depth and orientation of the protein in the membrane. (c) The final model that represents experimental data from NR at different contrasts, crystallographic, volumetric and chemical connectivity information, and thus describes the atomistic protein structure in the supported bilayer.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 74| Part 12| December 2018| Pages 1129-1168

https://doi.org/10.1107/S2059798318017503

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