Open AccessCrystallization and preliminary structural analysis of the Listeria monocytogenes Ca 2+ ‐ATPase LMCA1
Author(s) -
Andersen Jacob Lauwring,
Gourdon Pontus,
Møller Jesper Vuust,
Morth Jens Preben,
Nissen Poul
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911101548x
Subject(s) - listeria monocytogenes , crystallization , crystallography , molecular replacement , atpase , chemistry , ion , molecule , resolution (logic) , crystal (programming language) , crystal structure , biochemistry , biology , enzyme , bacteria , genetics , organic chemistry , artificial intelligence , computer science , programming language
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 P 2 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.