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Macromolecular Crystallography is a
technique used to study biological molecules such as proteins, viruses
and nucleic acids (RNA and DNA) to a resolution higher than ~5 Å. This
high resolution helps elucidate the detailed mechanism by which these
macromolecules carry out their functions in living cells and
organisms. Protein molecules can crystallize under regulated
conditions; the crystals are made up of multiple
copies of the molecule arranged in a regular 3-dimensional
lattice. The x-rays deflected ("scattered") by the atoms in equivalent
positions in the crystal lattice concentrate into sharp intense spots
(crystal diffraction pattern). The
macromolecular structure can be determined by analysis of the
intensities and positions of the diffraction spots.
The Macromolecular Crystallography
Group at the Stanford
Synchrotron Radiation Laboratory operates and develops
beamlines providing state of the art macromolecular crystallography
facilities and support for visiting researchers. Of the beamlines
currently operational, three (BL9-2, BL1-5 and BL14-1) are designed
for MAD experiments, two side stations (BL9-1, BL7-1 and BL11-1)
are also MAD capable at slightly reduced energy resolution. BL12-2,
with an undulator source, is optimized for microfocus applications,
but can also be used for conventional experiments (MAD,
screening, etc.). Researchers from universities, industry, and government
laboratories around the world can gain access to the beamline
facilities by submitting a research
proposal. Updates on beamline facilities and
other user information are posted to the px-ssrl
mailing list.
Beamlines are being prepared for the
2009-2010 User Run
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