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| Hiro Tsuruta - Molecular Envelope and Low-Resolution Crystallography | |
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Hiro Tsuruta
Stanford Synchrotron Radiation Laboratory, USA
We have adopted the key instrumental features of our small angle x-ray scattering instrument for recording single crystal diffraction data at very small angles (low-resolution). They make it possible to record the lowest index diffraction data of large protein complexes and virus particles.
With this type of data in hand, we have shown that a uniform-density solid sphere can be used to obtain a low-resolution molecular envelope of an icosahedral virus-like particle in a crystallographic unit cell. It has been shown that protein structures determined by solution x-ray scattering could also be used to accurately determine the exact position and orientation of a protein molecule in unit cell, a step critical in obtaining diffraction phases.
The low-resolution diffraction data have also been critical in determining crystallographic structures of large molecular assemblies in recent years.
This talk will outline the prospect of making effective use of low-resolution molecular envelope in macromolecular crystallography.
Date/time: Friday, 27 October, 9:50
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