Crystallization and Structure Determination Unit
The crystallization facility at the Structure Proteomics Unit utilizes several parallel approaches to determine and analyze the 3D structures of proteins and protein complexes. The aim of protein crystallization is to produce well-ordered protein mono-crystals large enough to diffract X-ray beams. The X-ray data are collected either on an in-house Liquid-Metal-Jet (LMJ) source or at a synchrotron facility, and are then used to solve the 3D structure of the protein.
Crystallization and Structural Determination Unit Activities
- Preliminary bioinformatics research: Providing assistance in planning the choice of constructs.
- Crystallization screening and optimization.
- Automated imaging for protein crystallization experiments.
- X-ray data collection on Liquid-Metal-Jet (LMJ) X-ray Diffraction System combined with pixel detector.
Screening for crystal quality by X-ray data diffraction.
In-situ screening of crystal quality on 96-well crystallization plate, at RT.
Data collection on single microcrystals at cryo temperature.
- Structure determination, refinement and evaluation.
- Structure analysis involves sequence-based-structure comparison with related proteins and correlation of the crystal structure with biochemical data so as to gain insight into its mode of action, specificity and biological relevance.
- Structure modeling of proteins, protein complexes and ligand binding.