structural biology

X-ray crystallography is a strong method for studying biomolecules’ 3D structure. Data gathering technologies for synchrotron radiation have improved, making this approach even more effective and efficient. The crystal is exposed to an intense stream of X-rays for getting high-resolution structural information. The protein crystals deflect these X-rays, resulting in dispersed beams and a diffraction pattern. The intensity and position of spots in the diffraction pattern allow the generation of an electron density map, which enable the identification of each atom in the protein as well as well as in any bound ligands and solvent molecules. Chemical bond lengths and angles may be determined with angstrom precision and a tenths of a degree, respectively, using this data. We can validate the location of a molecule’s contact with a protein, as well as how the chemical and protein are conformationally modified as a result of this interaction, using this information.