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The molecular architecture of N\u2010type ATPases is unknown and their biochemical properties and cellular functions are largely unexplored. We studied the\n                    <jats:italic>B. pseudomallei<\/jats:italic>\n                    N\n                    <jats:sub>1<\/jats:sub>\n                    N\n                    <jats:sub>o<\/jats:sub>\n                    \u2010type ATPase and investigated the structure and ion specificity of its membrane\u2010embedded c\u2010ring rotor by single\u2010particle electron cryo\u2010microscopy. Of several amphiphilic compounds tested for solubilizing the complex, the choice of the low\u2010density, low\u2010CMC detergent LDAO was optimal in terms of map quality and resolution. The cryoEM map of the c\u2010ring at 6.1 \u00c5 resolution reveals a heptadecameric oligomer with a molecular mass of ~141 kDa. Biochemical measurements indicate that the c\n                    <jats:sub>17<\/jats:sub>\n                    ring is H\n                    <jats:sup>+<\/jats:sup>\n                    specific, demonstrating that the ATPase is proton\u2010coupled. The c\n                    <jats:sub>17<\/jats:sub>\n                    ring stoichiometry results in a very high ion\u2010to\u2010ATP ratio of 5.7. We propose that this N\u2010ATPase is a highly efficient proton pump that helps these melioidosis\u2010causing bacteria to survive in the hostile, acidic environment of phagosomes.\n                  <\/jats:p>","DOI":"10.15252\/embr.201643374","type":"journal-article","created":{"date-parts":[[2017,3,10]],"date-time":"2017-03-10T21:05:26Z","timestamp":1489179926000},"page":"526-535","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":45,"title":["Molecular architecture of the N\u2010type ATPase rotor ring from Burkholderia pseudomallei"],"prefix":"10.1038","volume":"18","author":[{"given":"Sarah","family":"Schulz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Wilkes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deryck J","family":"Mills","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2013-4810","authenticated-orcid":false,"given":"Werner","family":"K\u00fchlbrandt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3364-3320","authenticated-orcid":false,"given":"Thomas","family":"Meier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2017,3,10]]},"reference":[{"key":"BFEMBR201643374_CR1","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1146\/annurev-biochem-060614-034124","volume":"84","author":"W Junge","year":"2015","unstructured":"Junge W, Nelson N (2015) ATP synthase. 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