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X-ray Crystallography Core Laboratory


The X-ray Crystallography Core Laboratory provides intramural researchers with 3-dimensional structural characterization using molecular biology, biochemistry, and X-ray crystallographic techniques on biological systems.


The crystal structure of Ara h 2 (green) was obtained as a fusion molecule with the maltose protein (magenta)
The crystal structure of Ara h 2 (green) was obtained as a fusion molecule with the maltose protein (magenta).

What is X-ray Crystallography?

Macromolecular crystallography is used to obtain 3-dimensional models of large proteins, protein-DNA or protein-protein complexes. These structures can provide detailed information of how proteins bind ligands, function, or interact with one another.

To solve these structures, we first crystallize the molecules of interest by screening them against an array of solutions with different properties. When crystals are obtained, we expose them to X-rays from an in-house X-ray source or synchrotron radiation to obtain diffraction images on sensitive X-ray detectors. The diffraction spots collected from these images can be used to back calculate the relative locations of the atoms to one another in the crystal to obtain a 3-dimensional model of the macromolecule sample. Information obtained from structures can be used to guide future biological experiments, such as site directed mutagenesis or drug design.

NIEHS Shared and Core Facilities are available to NIH researchers. Information for staff on utilizing these services may be found on the NIEHS Junction or by contacting the staff below.

Scientific Staff

Lars C. Pedersen, Ph.D.
Lars C. Pedersen, Ph.D.
Director, X-ray Crystallography Core Laboratory
P.O. Box 12233
Mail Drop F3-09
Durham, N.C. 27709

Tel 984-287-3538