Structural Investigation of Transmembrane Proteins by Single Particle Cryo-EM and X-Ray Crystallography

Protein crystals of a bacterial Ca2+ exchanger.


Transmembrane proteins play an important role in many signaling pathways and the exchange of material across the membrane. Many are considered to be are important pharmaceutical targets.
 The intracellular concentration of calcium ions controls multiple physiological processes, such as muscle contraction, cell proliferation, and release of neurotransmitters. Diverse Ca2+ transporters and pumps act in concert to restore the low resting concentration of calcium (~100nM) in order to prevent damage to the cell due to Ca2+ overload. By analyzing the 3-D structure a Ca2+-antiporter we are trying to obtain a better understanding of how cells establish the Ca2+ resting concentration. In a collaborative effort, we are also investigating the structure of a transporter complex.

Related Publications+-

Related Publications

Project Lead-+

Project Initiator+-

Mark Hilger

Supervisor until Aug. 2015 





Henning Stahlberg

Key Publication+-

Key Publication


Protein Crystallization Center - PCC (UZH)

Swiss Lightsource SLS (PSI)

Philips CM10

Philips CM200FEG