Protein Crystallography refers to X-ray diffraction analysis of single crystals of organic molecules such as proteins, viruses, or protein complexes. This fast and accurate technique determines 3D macromolecular structure at near atomic resolution, enabling the detection of molecular interactions, a critical capability in fields such as rational drug design.

The final structure determination of organic crystals is typically carried out at synchrotron facilities but prior data acquisition in the laboratory with good accuracy and high throughput is critical. Consequently, X-ray laboratory installations require a highly intense monochromatic beam with a moderate divergence (typically 4 mradians) of X-ray radiation to illuminate the crystal.

In the recent years microfocussing sealed sources became more and more popular even or this high demanding application since performances are now superior to tradition Rotating Anode Generators (RAG) for large and small crystals.

Application notes hereunder provide detailed performances for traditional protein crystallography on various samples and sulfur SAD phasing and performance comparisons of GeniX our beam delivery system with traditional Rotating Anode Generators.