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DOE Pulse

Revealing protein structures at record pace

Representation of the nine-gene operon in (A) the cyanobacteria Synechocystis 6803 and (B) other cyanobacteria.






Representation of the nine-gene
operon in (A) the cyanobacteria
Synechocystis 6803 and
(B) other cyanobacteria.

Determining the precise structure of a protein can take years, but a high-throughput protein pipeline developed by researchers working at DOE's Lawrence Berkeley National Laboratory’s Advanced Light Source could help scientists keep pace with the flood of data from far-ranging genomic studies. The SIBYLS beamline employs small angle x-ray scattering (SAXS) to image proteins in their natural states, without the need for crystallization. The 10-angstrom resolution is nowhere near that of x-ray crystallography, but it’s often sufficient to solve structures through analogy with known proteins or by eliminating models that don’t fit. And SAXS makes up for its lack of precision with accurate information on shape, assembly, and conformational changes of proteins in solution.

[Paul Preuss, 510.486.6249,
paul_preuss@lbl.gov]