I'm working on a physical chemistry project that is a report on a paper that uses X-ray crystallography to characterize a protein. So I am studying X-ray crystallography more in depth than the book introduces, and I have a few questions that I couldn't really find answers to online. 1. How does measuring more diffraction peaks improve resolution? Does that mean a LARGER crystal improve resolution? (I don't think it's that simple...) 2. How is the resolution defined? People online seem to say that the limit is wavelength/2, but I'm having trouble deriving it from the Bragg Law (I think a larger diffraction angle means higher resolution?) 3. Regarding the unit cell, do you just "choose" the shape and dimensions of the unit cell (square, triangular, oblique, etc.) as long as it contains at least one of each atom of your molecule? How does this choice affect the resolution? 4. This is pretty much a technical question: How do detergents interrupt crystallization? Thank you!