Studies of protein structures by X-ray diffraction

	Areas of Research - Examples
	Studies of Liquids
	Electronic Structure and Dynamics      of Surface Systems
	Studies of Reactions at Surfaces
	Surface structure, dynamics & magnetism
	Studies of surfaces with X-ray diffraction
	Environmental and materials research
	Studies of Protein Crystals
	Studies of Molecule Structures      with SAXS
	Microscopes - IR & PEEM
	Accelerator Physics
	Nuclear Physics
	Activity Reports from MAX-lab
	Seminars at MAX-lab
	Go to start Research at MAX-lab

In present day biology and biochemistry, the information on protein structure and function generated by structural biology plays an extremely important role in our understanding of fundamental life processes and of the pathology of disease. It is only the three dimensional structures of biological macromolecules that give full insight into their function and their ability to interact with other molecules. Furthermore structural biology plays an important role in disciplines such as biotechnology and drug design. The accurately determined three-dimensional structure of an enzyme involved in a disease is an absolute prerequisite for structure based drug design, one of the most powerful tools in modern pharmaceutical research.

The most common techniques for determining three-dimensional (3D) structures of biological macromolecules at atomic detail are X-ray crystallography and NMR spectroscopy. X-ray crystallography has been responsible for about 85% of all biomolecular structures deposited in the Protein Data Bank (PDB, http://www.rcsb.org/pdb). Recent technological and methodological advances have opened the field to a wide range of new problems. X-ray crystallography is in principle applicable to the complete spectrum of biological macromolecules, derived from all organisms (from eubacteria and archaeae to human) and of all sizes (from small domains to gigantic ribosome or virus particles).

Most X-ray crystallography of biological molecules occurs nowadays at synchrotron radiation sources. While around 1990 most 3D structures of biological macromolecules were still solved using X-ray laboratory sources, the importance of synchrotron radiation can nowadays no longer be denied. The fraction of deposited structures in the PDB for which data was collected at a synchrotron radiation source rose from 28% in 1992 to over 85% in 2007. The advantage of being both a high intensity X-ray provider and the fine tuneability of the wavelength makes synchrotron radiation sources the optimum choice for biological X-ray crystallography.

At I911 there is three beamlines for X-ray crystallography of biological molecules (often also referred to as macromolecular crystallography or MX): I911-2, I911-3 and I911-4 (or collectively called I911-MX). At I911-3 the X-ray wavelength can be changed which is very important for being able to solve structures with only small resemblances to already known structures. I911-3 also has an industrial robot that is used to increase the scientific output of the beamline. The fixed wavelength stations I911-2 and I911-5 are important workhorses for crystallographic experiments where wavelength tuneability is not important.

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