Crystallography is pretty much using X-rays to make an atomic microscope. We use X-rays because their wavelength is similar to the length between an atomic bond. This means X-rays scatter off them and we can make a 3D model of a protein or other molecules that we crystallise. The problem is that you can’t focus X-rays with a lense like you do a regular microscope so we have to do some fancy tricks with maths and computers to turn the scattered X-rays into an image. So a synchrotron, where we get these X-rays, is effectively a huge microscope that needs focusing.
Crystallography is the study of crystal structure.
We first need to understand what are crystals: they are formed by many copies of the same molecule all oriented in the same way, at the same distance of each other, and concentrated in a small volume. This gives crystals interesting properties, that we can measure and relate to the structure of the molecules inside. That is what crystallography is!
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