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Poul Nissen

Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1

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Ca(2+)-ATPases are ATP-driven membrane pumps that are responsible for the transport of Ca(2+) ions across the membrane. The Listeria monocytogenes Ca(2+)-ATPase LMCA1 has been crystallized in the Ca(2+)-free state stabilized by AlF(4)(-), representing an occluded E2-P(i)-like state. The crystals belonged to space group P2(1)2(1)2 and a complete data set extending to 4.3 Å resolution was collected. A molecular-replacement solution was obtained, revealing type I packing of the molecules in the crystal. Unbiased electron-density features were observed for AlF(4)(-) and for shifts of the helices, which were indicative of a reliable structure determination.
Original languageEnglish
JournalActa Crystallographica. Section F: Structural Biology and Crystallization Communications Online
IssuePt 6
Pages (from-to)718-22
Number of pages5
Publication statusPublished - 2011

    Research areas

  • Calcium-Transporting ATPases, Crystallization, Crystallography, X-Ray, Listeria monocytogenes, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary

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