X-Ray diffraction Automated crystallization set up facility Automate crystal visualization camera.

• X-Ray diffraction
• Automated crystallization set up facility
• Automate crystal visualization camera

Working Princple

In the present world of science, X-ray crystallography is the most widely used technique for determination of structures of biological macromolecules. This technique allows us to determine macromolecule structures that provides a detailed understanding of the interactions occurring at the molecular levels. Structure based drug design, study of protein-ligand interactions and structure-function relationships are the major fields where X-ray crystallography acts as a major tool. X-Ray crystallography is an experimental technique that exploits the fact that X-rays are diffracted by crystals as they have a wavelength (in Å ~10-10 m) corresponding to the size of an atom

Principle of X-ray diffraction

Each crystal has its unit cell parameters (a,b,c and α, β, γ) and in a crystal lattice infinite sets of plane can be drawn from the lattice points. These planes can be considered as source of diffraction and designated by set of miller indices. According to Braggs laws, when a wavelength (λ nm) with an angle θ passes through a crystal (which has a set of equivalent planes with hkl) a diffracted beam with the same angle is produced from which we can calculate the d spacing of the planes.

Bragg's law

                nλ = 2dsinθ

                Where    n : Order of diffracted beam
                              d : Spacing between two adjacent planes of atoms
                              λ : Wavelength of incident X-ray
                              θ : Angle of incidence of X-ray

The sets of d and intensities from protein crystals come in a unique diffraction pattern.