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

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.