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Course - Cold Spring Harbor, NY, United States

 

Crystallography and X-ray diffraction yield a wealth of structural information unobtainable through other methods. 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 and complexes), crystal characterization, X-ray sources and optics, synchrotrons, Cryocrystallography, data collection, data reduction, heavy atom substructure determination, multiple isomorphous replacement, single and multiwavelength anomalous diffraction, molecular replacement, solvent flattening, non-crystallographic symmetry averaging, electron density interpretation, molecular graphics, structure refinement, structure validation, coordinate deposition and structure presentation.

Participants learn through extensive hands-on experiments in fully equipped labs. Participants will crystallize multiple proteins and determine their crystal structures by several methods while learning through extensive lectures on Crystallographic theory and informal discussions behind the techniques. Applicants should be familiar with the creation and editing of simple text files on Linux workstations using a screen based editor (either vi or emacs).

Organization: Cold Spring Harbor Laboratory

 

 

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