|
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 five
beamlines currently operational, two (BL9-2 and BL1-5) are designed
for MAD experiments, two side stations (BL9-1 and BL11-1) are also
MAD capable at slightly reduced energy resolution and one (BL11-3)
operates at a fixed energy above the Se K edge. BL7-1 is available
to users in monochromatic mode; energy tunability will be
implemented in 2008. 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.
|
