Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria monocytogenes

Abstract

Ca2+-ATPases are members of a large family of membrane proteins that maintain the selective movement of cations across biological membranes. A putative Listeria monocytogenes Ca2+-ATPase (Lmo0818) was crystallized in an unknown functional state. The crystal belonged to space group P212121 and a complete data set was collected to 3.2 Å resolution. The molecular-replacement solution obtained revealed that Lmo0818 is likely to adopt an E2-­like state mimicking the phosphorylated intermediate in the functional cycle of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and a stacked bilayer `type I' packing in the crystal. This research was originally published in Acta Crystallographica Section F: Structural Biology and Crystallization Communications. © International Union of Crystallography