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 ~5Å. 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 Lightsource operates and develops beamlines providing state of the art macromolecular crystallography facilities and support for visiting researchers. Of the beamlines currently operational BL9-2 and BL14-1 are designed for MAD experiments; the side station BL7-1 is also MAD capable at slightly reduced energy resolution. BL12-1 and BL12-2, with an undulator source, are 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 here.

• Save the dates: The course RapiData 2024 on Data Collection and Structure Solving will take place from April 29 to May 4, 2024 and we are back in-person!. See the course announcement for more information. Application deadline: January 31, 2024.

• New BAG Proposal Option: Click here to learn more about all beamtime proposal mechanisms.

• RADDOSE-3D in the BluIce Collect Tab.

• New Helical Collection sub-tab in Collect tab with shutterless helical collection on beamlines 12-1 and 12-2.
• Diffraction Quality Strip chart in Collect tab.
• Remote access to room temperature/crystal dehydration experiments on 12-1.
• New Eiger 16M detector on beamline 12-2 and Pilatus 6M detector on beamline 14-1.

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