X-Ray diffraction is the only method currently available for the determination of the detailed three-dimensional structure of macromolecules. In this article, the principles behind the use of X-ray crystallography in the study of protein structure are presented. The results obtained in its application to several enzymes are discussed, as well as the limitations of the method.

The host-guest interaction of a series of cyclohexyl-appended guests with cucurbit[8]uril (Q[8]) was studied by ¹H NMR spectroscopy, isothermal titration calorimetry (ITC), and X-ray crystallography. The X-ray structure revealed that two cycloalkane moieties can be simultaneously encapsulated in the hydrophobic cavity of the Q[8] host to form a ternary complex for the first time.

A new detector system for protein crystallography is now being developed based on an X-ray HARP-FEA (high-gain avalanche rushing amorphous photoconductor-field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche effect with a single driven FEA has several advantages over currently available area detectors, ...

Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the aut...

Vascular endothelial growth factors (VEGFs) regulate blood and lymph vessel development upon activation of three receptor tyrosine kinases: VEGFR-1, -2, and -3. Partial structures of VEGFR/VEGF complexes based on single-particle electron microscopy, small-angle X-ray scattering, and X-ray crystallography revealed the location of VEGF binding and domain arrangement of individual receptor subdoma...

Free energy landscapes decisively determine the progress of enzymatically catalyzed reactions. Timeresolved macromolecular crystallography unifies transient-state kinetics with structure determination because both can be determined from the same set of X-ray data. We demonstrate here how barriers of activation can be determined solely from five-dimensional crystallography. Directly linking mole...

Recently introduced electronic area X-ray detectors (such as CCD based detectors) are having an enormous impact within the experimental x-ray community. The efficiency and ease of data collection has been improved considerably. They are also making practical the implementation of powerful new methodologies in data collection such as fine rotation slicing of crystallography data or multi-wavelen...