X-RAY METHODS IN STRUCTURAL BIOLOGY
October 13 - 28, 2008
Application Deadline: June 15, 2008

Instructors:
William Furey, V.A. Medical Center, Pittsburgh
Gary Gilliland, Centocor, Inc.
Alexander McPherson, University of California, Irvine
James Pflugrath, Molecular Structure Corporation, Texas

Crystallography and X-ray diffraction yield a wealth of structural information unobtainable through other methods. This intensified 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, crystal freezing, data collection, data reduction, multiple isomorphous replacement, 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. One or more proteins are crystallized and the structure(s) determined by several methods, in parallel with lectures on the 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).

Speakers in the 2007 course included:


This course is supported with funds provided by the National Cancer Institute & the Howard Hughes Medical Institute