Small-angle scattering gives direct structural information about a membrane protein inside a lipid environment

TY - JOUR

T1 - Small-angle scattering gives direct structural information about a membrane protein inside a lipid environment

AU - Kynde, Søren Andreas Røssell

AU - Skar-Gislinge, Nicholas

AU - Pedersen, Martin Cramer

AU - Midtgaard, Søren Roi

AU - Simonsen, Jens Baek

AU - Schweins, Ralf

AU - Mortensen, Kell

AU - Arleth, Lise

PY - 2014/2

Y1 - 2014/2

N2 - Monomeric bacteriorhodopsin (bR) reconstituted into POPC/POPG-containing nanodiscs was investigated by combined small-angle neutron and X-ray scattering. A novel hybrid approach to small-angle scattering data analysis was developed. In combination, these provided direct structural insight into membrane-protein localization in the nanodisc and into the protein-lipid interactions. It was found that bR is laterally decentred in the plane of the disc and is slightly tilted in the phospholipid bilayer. The thickness of the bilayer is reduced in response to the incorporation of bR. The observed tilt of bR is in good accordance with previously performed theoretical predictions and computer simulations based on the bR crystal structure. The result is a significant and essential step on the way to developing a general small-angle scattering-based method for determining the low-resolution structures of membrane proteins in physiologically relevant environments.

AB - Monomeric bacteriorhodopsin (bR) reconstituted into POPC/POPG-containing nanodiscs was investigated by combined small-angle neutron and X-ray scattering. A novel hybrid approach to small-angle scattering data analysis was developed. In combination, these provided direct structural insight into membrane-protein localization in the nanodisc and into the protein-lipid interactions. It was found that bR is laterally decentred in the plane of the disc and is slightly tilted in the phospholipid bilayer. The thickness of the bilayer is reduced in response to the incorporation of bR. The observed tilt of bR is in good accordance with previously performed theoretical predictions and computer simulations based on the bR crystal structure. The result is a significant and essential step on the way to developing a general small-angle scattering-based method for determining the low-resolution structures of membrane proteins in physiologically relevant environments.

U2 - 10.1107/s1399004713028344

DO - 10.1107/s1399004713028344

M3 - Journal article

SN - 0907-4449

VL - 70

SP - 371

EP - 383

JO - Acta Crystallographica. Section D: Biological Crystallography

JF - Acta Crystallographica. Section D: Biological Crystallography

IS - 2

ER -