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Volume 545 Issue 7653, 11 May 2017

The cover shows lipid bilayers in crystals of a calcium pump as revealed by X-ray solvent contrast modulation. Conventional X-ray crystallography cannot visualize membrane phospholipids, so structure analyses of membrane proteins usually have to pretend that no lipid bilayer exists. In this issue, Chikashi Toyoshima and colleagues reveal a crystallographic method using solvent contrast modulation that is able to include phospholipid head groups, signalling that future crystallography images no longer have to be fat-free. They deployed their technique on four states of a calcium pump, revealing for the first time how the lipid bilayer actively participates in the successive conformational switches of the pump. They were able to define a belt of tryptophan residues, which functions as a ‘membrane float’, allowing the whole pump axis to tilt with respect to the membrane bilayer during ion transport, as well as arginine and lysine residues, which act as ‘membrane anchors’ and provide leverage for the helix movements. Credit: Yoshiyuki Norimatsu and Chikashi Toyoshima

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