X-ray Diffraction Applications – Proteins 

X-ray crystallography is the only structural biology technique that allows us to “see” details of molecular structure at the atomic level. Over the last few decades many structures of proteins, nucleic acids and macromolecular complexes have been determined, providing structural insights into the function of basic building blocks of living organisms.

Novel structures

X-ray diffraction data is collected on high-precision diffractometers, like Agilent’s SuperNova, and used to determine three-dimensional structures of important biological macromolecules such as proteins and nucleic acids. These structures are used to deepen our understanding of biological processes at the atomic level. Information about the structure and dynamics of these macromolecules can be used to design new medicines.

Crystal screening

Some macromolecular crystals are too small or diffract X-rays too weakly to allow in-house data collection; experiments require synchrotron radiation. In such cases in-house diffractometers such as the SuperNova can be used for the initial characterisation of crystals and to select the best samples for synchrotron data collection.

In situ testing of macromolecular crystals

Protein crystals are fragile and difficult to handle. Successful structure determination can be improved if you can test the diffraction properties of crystals and chose the suitable ones for further analysis before they are removed from their original crystallization drops. Agilent’s PX Scanner is a unique instrument that allows you to perform such in situ testing experiments and helps to speed up crystallography projects.

Ligand binding