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Integrated Structural Biology Grenoble
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Contact person(s) related to this article / DUPEUX Florine

High Throughput Membrane Protein Crystallisation

Presentation

The High Throughput Membrane Protein (HTMPC) platform fused with HTX Lab (EMBL) to give rise to a unique membrane protein crystallization platform. The platform is fully equipped to accomplish successful crystallization of your membrane protein (in meso, bicelle, vapor diffusion). Robotic systems nanovolume dispenser (Mosquito TTPLabtech) allows to screen 96 precipitant conditions with small amount of sample (5-10 µl per plate) in less than 10 minutes. Our platform works with commercially available kits specialized in membrane protein crystallization. An automated imaging system, RockImager 1500 (Formulatrix), visualizes crystallization drops with visible, polarized and UV lights, which allows a better identification of protein crystals. The smallest crystals which can be confidently detected are about 10 micrometers.

The diffusion rate and mobile fraction of the membrane protein can be determined by FRAP (Formulatrix), that allows to identify the optimal conditions for LCP crystal growth.

Key words

Structural Biology, high-throughput crystallization, in meso crystallization, membrane proteins, lipidic cubic phase; LCP-FRAP

Contact

htx embl.fr

Dedicated staff

  • Dupeux Florine

Specific equipment

Robot for in meso membrane protein crystallization (nanodispenser), automated system for imaging crystallization plates, UV microscope for visualisation of protein crystals, temperature controlled rooms for crystallisation (20°C, 4°C), CRIMS to visualize images through internet.

Access mode

Open access to internal and external users.
https://www-crims-htmpc.ibs.fr
(login: crimsUser; pwd: 6horowitz)

Cost

HTMPC-COST

Location

PSB/Room S06
PSB/Office 120

How to make a request?

Register and send request forms on our website: https://www-crims-htmpc.ibs.fr
(login: crimsUser; pwd: 6horowitz)

Credits

In the general case users must aknowledge the platform in their publications: “This work used the platforms of the Grenoble Instruct-ERIC center (ISBG ; UMS 3518 CNRS-CEA-UGA-EMBL) within the Grenoble Partnership for Structural Biology (PSB), supported by FRISBI (ANR-10-INBS-0005-02) and GRAL, financed within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS (ANR-17-EURE-0003)."