Structural Analysis of Biomacromolecules

Research

• The department deals with x-ray structure analysis of biological macromolecules. We are mainly interested in detailed studies of proteins or protein complexes and ligands and their function but also in other crystallisable macromolecules. Protein samples are mostly prepared in collaboration with other laboratories.
  

• Systematic analysis of interactions between proteins and synthetic polymers utilized in biomedical applications.

Methods

• Protein crystallography. X-ray structure analysis of macromolecules. Purification, crystallization, single crystal X-ray data collection and solution of 3D molecular structure.
• Additional methods: study of properties of macromolecules in solution, development of crystallization screens, computer simulations - molecular dynamics, classification and database development.

Fig. 1: A schematic representation of the structure determination process: single crystals of enzyme laccase, X-ray diffraction image, and a detail of structure of the studied enzyme: blue mesh - electron density contour, yellow sticks - interatomic bonds.

• Extracelular domains of natural killer cell receptors of immune system (collaboration partners: IMB AS CR, v.v.i. and the Charles University)
• Industrially exploitable oxidoreductases (collaboration: Novozymes A/S)
• Enzymes not characterized so far (two domain laccase)
• Enzymes operating on DNA/RNA
• Systematic structural study of immunoglobulins
• Complex of chitinolytic enzymes from bacteria of intestinal microflora (collaboration: IAPG AS CR, v.v.i.)
• Cold active beta-galactosidase (collaboration: Institute of Chemical Technology, Praha)
• HIV-1 protease and its interaction with inhibitors, structural effects of drug-induced mutations (collaboration: IOCB AS CR)
• Protein - polymer interactions (in collaboration with several European laboratories) 
• Equipment for characterization, purification and crystallization of biological macromolecules, and for cryogenic storage of protein crystals
• Computer and software equipment for x-ray data collection, determination of 3D structure and analysis
• X-ray diffraction experiments are realized at the Institute of Physics ASCR, Biotechnology Institute AS CR, IOCB ASCR and European synchrotron light sources (Bessy II – Helmholtz Zentrum Berlin, ESRF Grenoble, Elettra Trieste).

  Fig. 2: Two perpendicular views of a hexamer of the enzyme catalysing hydrolysis of lactose.   This macromolecular complex of beta-galactosidase from Arthrobacter sp. C2-2 represents information about spatial arrangement of 55000 non-hydrogen atoms of this cold-active enzyme.

More information about the department
Web page:     http://protein.awardspace.com/