Cover: The cover shows the 3D structure of the Burkholderia pseudomallei N‐type ATPase membrane‐embedded rotor analyzed by electron cryo‐microscopy, with a cryo‐EM image in the background showing the single particles used for reconstruction. The membrane protein complex is from a “novel, next to” N‐type rotary ATPase, which has been found to accompany conventional F‐type ATP synthases in some microorganisms. The B. pseudomallei rotor consists of 17 c‐subunit copies forming the rotor, with each rotor blade able to reversibly bind one proton. This makes this rotary ATPase a highly efficient proton pump, which is proposed to counteract acid stress and keep pH homeostasis in phagosomes during the infection process of host cells. From Sarah Schulz, Martin Wilkes, Deryck J Mills, Werner Kühlbrandt and Thomas Meier: Molecular architecture of
the N‐type ATPase rotor ring from Burkholderia pseudomallei. For detail, see Scientific Report on page 526. Scientific images by Martin Wilkes, Deryck Mills, Sarah Schulz, Werner Kühlbrandt and Thomas Meier (Imperial College London and Max Planck Institute of Biophysics, Frankfurt).