Malcolm Capel
Cornell University, NY·Biophysics
To understand how a protein, enzyme or virus works, biologists often need to see where its atoms sit. The standard way is macromolecular crystallography: grow a crystal of the molecule, shine an intense X-ray beam through it, and reconstruct the three-dimensional structure from the diffraction pattern.
- Fields
Biophysics
Biochemistry
Physics
- Topics
macromolecular crystallography
X-ray diffraction
synchrotron
- Grants
- 1 known grant, through Mar 2028
What they work on
- Provide and staff round-the-clock on-site and remote user access to two macromolecular crystallography beamlines at the Advanced Photon Source, including training and outreach by staff scientists.
- Maintain beamline hardware and software at peak performance, covering motion control systems, vacuum and ultrahigh vacuum pumps, monochromator cryopumps, compute clusters, storage and network infrastructure.
- Upgrade beamline optics and instrumentation, installing a ganged channel-cut monochromator on 24-ID-C and new MD3 goniometers on both beamlines in step with the Advanced Photon Source upgrade shutdown.
- Extend the RAPD automated data collection and analysis software with externally developed processing routines and new methods for routine serial microcrystallography and fully automated, unassisted crystal screening and data collection.
More about the research
That requires a synchrotron, a facility that produces X-ray beams far brighter than any lab source. This project operates and continuously rebuilds the user-facing side of two such beamlines at the Advanced Photon Source, run by the Northeastern Collaborative Access Team (NE-CAT), so that researchers anywhere can collect structural data.
Why it matters
Atomic-resolution structures underpin how researchers explain enzyme mechanisms and design drugs, but few groups can build or run a synchrotron beamline. Keeping these two beamlines current, staffed and remotely accessible gives the structural biology community a route to data from small or poorly behaved crystals, and the automation and serial microcrystallography methods developed here could lower the expertise barrier for new users.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Mark Schlossman
University of Illinois Chicago, IL·Chemistry
Design and build a second beamline at ChemMatCARS, with two experimental stations fed by an independent superconducting undulator, the magnet device that generates the X-ray beam, doubling available beamtime.
Vukica Srajer
University of Chicago, IL·Biophysics
Install and test new hardware to generalize Electric-Field Stimulated X-ray crystallography, in which strong external electric fields induce motions in protein crystals that are then recorded by X-ray diffraction at atomic resolution.
Gloria Borgstahl
University of Nebraska Medical Center, NE·Biochemistry
Map the proton environment of human MnSOD, an antioxidant enzyme, in its resting reduced and oxidized manganese states, using neutron crystallography at Oak Ridge National Laboratory to locate hydrogen atoms.
The school
Cornell University: 37 labs on PI Pages, $1.6B a year on research, 537 research doctorates a year.
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