X-ray crystallography has been the cornerstone of Structural Biology for half a century. This intense laboratory/computational course focuses on the major techniques used to determine the three-dimensional structures of macromolecules. It is designed for scientists with a working knowledge of protein structure and function, but who are new to macromolecular crystallography. Topics to be covered include basic diffraction theory, crystallization (proteins, nucleic acids, complexes and membrane proteins), synchrotron X-ray sources and optics, data collection and processing, structure solution by experimental phasing methods (SAD, MAD, MIR, and others) and molecular replacement, electron density maps improvement (solvent flattening, non-crystallographic averaging, etc.), model building and refinement, structure validation, coordinate deposition and structure presentation. In addition, the course will for the first time extend to the theory and computation for small angle X-ray scattering (SAXS) and single particle cryoelectron microscopy.
Participants learn through extensive hands-on experiments in fully equipped labs, crystallize multiple proteins and determine their crystal structures by several methods while learning through extensive lectures on theory. Informal discussions behind the techniques are frequent and students will be responsible also for collecting questions to be answered in specific sessions.
Applicants should be familiar with the creation and editing of simple text files on Linux workstations using a screen based editor (e.g. vim or emacs).