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Updated: Jun 1, 2026

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Crystallization and preliminary structural analysis of the Listeria monocytogenes Ca(2+)-ATPase LMCA1
Jacob Lauwring Andersen1, Pontus Gourdon, Jesper Vuust Møller
1Centre for Membrane Pumps in Cells and Disease-PUMPKIN, University of Aarhus, Gustav Wieds Vej 10C, Aarhus C, Denmark.
Abstract:
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.

