Related Experiment Video
Updated: May 23, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Purification, crystallization and preliminary crystallographic studies of a PacL homologue from Listeria
Kim Langmach Hein1, Poul Nissen, Jens Preben Morth
1Centre for Molecular Medicine Norway, University of Oslo, PO Box 1137 Blindern, 0318 Oslo, Norway. kimlan@ncmm.uio.no
Abstract:
Ca(2+)-ATPases are members of a large family of membrane proteins that maintain the selective movement of cations across biological membranes. A putative Listeria monocytogenes Ca(2+)-ATPase (Lmo0818) was crystallized in an unknown functional state. The crystal belonged to space group P2(1)2(1)2(1) 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 Ca(2+)-ATPase (SERCA) and a stacked bilayer `type I' packing in the crystal.
