Possibilities for biomacromolecular crystallization at BIC Core Facility at CEITEC, Brno

Josef Houser, Michaela Wimmerová

CEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00 Brno, Czech Republic, bic@ceitec.cz, josef.houser@ceitec.cz


Protein crystallization followed by X-ray diffraction is well established method for determination of the protein structure. It is historically the first technique developed and lead to determination of more than 93 000 deposited structures of proteins and their complexes up to date [1]. It is currently the only method that enables atomic resolution for structures of virtually unlimited size including proteins, nucleic acids and their various complexes.

We offer a wide range of crystallization techniques in the Biomolecular Interaction and Crystallization (BIC) Core Facility at CEITEC MU in Brno. The standard 96-well crystallization screening plates are set up by Mosquito (TTP Labtech) and Phoenix (Rigaku) robotic systems allowing for high throughput, precision and accuracy. The optimization of crystallization conditions is further simplified by Dragonfly (TTP Labtech) pipetting robot. The automation speeds up the whole process allowing to set up 1000 – 2000 different conditions with 100 ul of concentrated sample in one hour. The storage and crystal tracking is ensured by Minstrel HT (Rigaku) equipped with UV detection and advanced software analysis.

Beside standard sitting/hanging drop crystallization screening, we are using specialized techniques of crystallization under oil or in capillaries. TG40 machine (Centeo) serves for temperature optimization screening. We also offer a wide range of additives and nucleants as well as heavy atom compounds for protein derivatization. Recently we broaden the spectrum of available methods by membrane proteins crystallization in cubic and sponge phase thanks to Mosquito LCP machine (TTP Labtech). Biophysical properties of the samples can also be determined using analytical ultracentrifugation, dynamic light scattering and CD spectroscopy available to users.

All the possibilities are available not only to research groups in CEITEC, but thanks to Open access grant also to any non-commercial users worldwide for free (in 2015).


The running of the Core Facility Biomolecular Interaction and Crystallization is supported by the European Union under the Seventh Framework Programme by CEITEC (CZ.1.05/1.1.00/02.0068) project from European Regional Development Fund and Open access project by Czech Ministry of Education (LM2011020).


1.         http://pdb.rcsb.org. H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne (2000) The Protein Data Bank. Nucleic Acids Research, 28: 235-242