About Protein Crystallography: From Purified Protein to Validated Structure

You will learn how an atomic model of a protein is produced from a purified sample: how crystals are grown through controlled supersaturation, how a crystal lattice diffracts X-rays according to Bragg's law, and how diffraction intensities relate to the electron density through the Fourier transform. You will understand why the phase problem exists and how molecular replacement, anomalous dispersion, and isomorphous replacement solve it. You will finish able to read a structure critically — resolution, R-free, B-factors, Ramachandran and clash outliers — and to judge when single-particle cryo-EM is the better experiment.

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