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. Rotating Anodes coupled to confocal multilayer optics are the standard beam delivery systems for Protein Crystallography.

By using the FOX2D optics one can characterize large membrane protein crystals using high throughput, and also succeed in screening tiny or very weekly diffracting samples, all the while being capable of analyzing long-unit cell crystals. Xenocs FOX2D optics are the most cost effective solutions for significantly improving the throughput and resolution of laboratory X-ray installations, and lead to higher flux and intensity and better merging statistics (I/σ, Rsym). Application notes hereunder provide detailed performance comparisons of our optics with other solutions available on the market.