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X-Ray Crystallography

Jörg Labahn has continously worked on the methods of membrane protein research. In addition, his group investigates the crystallographic structure solution of human membrane proteins, which are of neuro-scientific interest or relevant in infection biology.

A major goal for the next years is to analyze membrane protein structures. In particular, Labahn focuses on developing an approach which allows collecting in-situ diffraction data from crystals obtained with his in-meso-phase crystallization method.

In-meso-phase crystallization

The lipidic meso-phases (Pn3m, Ia3d, Lα, Lc) are formed by monoolein with different amounts of water. The formation of these crystalline phases can be monitored by change of optical properties. Phase formation in the presence of membrane protein leads to insertion oft protein into the hydrophobic layers of the monoolein. In case of the cubic phases (Pn3m, Ia3d) 3-dimensional diffusion of the protein within the membrane-like layer is possible: The crystalline meso-phase acts as a solvent for the membrane protein.

Reducing the water content of meso-phase by vapor diffusion induces crystallization (phase separation) of the membrane protein. J. Kubicek, et al. PlosOne 7(4): e35458 (2012).

CIMP optimization of crystallization conditions

One of the major obstacles in the structural analysis of human membrane proteins is the optimization from a 1st-hit (left) to diffracting crystals (right).