Eaton E. Lattman, Ph.D.
Hauptman-Woodward Institute
Principal Research Scientist
Chief Executive Officer and Executive Director Emeritus

B.A., Chemistry and Physics, Harvard College, 1962
Ph.D., Biophysics, Johns Hopkins University, 1969
Medical Research Institute
700 Ellicott Street
Buffalo, NY 14203-1102
Tel : (716) 898-8612
Fax: (716) 898-8660

Research Interests - current

• Use of x-ray free-electron lasers in imaging biological structures
• Development and improvement of methods in protein crystallography
• Drug Design

Research Interests - career
During his career Eaton Lattman has worked on a number of major research themes, two of which are summarized below.

  • Research Methods in Protein Crystallography.
    • Lattman made significant contributions to molecular replacement. This is a method in which knowledge of the structure of a related molecule greatly facilitates the crystal structure determination of a particular molecule of interest. It is often used, for example, when the structures of a series of mutants of a molecule is of interest. He wrote a rotation function program that was in common use for at least a decade. That program introduced a new set of locally orthogonal angles for representing the orientation of molecules (or other objects in space). The angles are widely used in many programs today. With Robert Kretsinger he carried out the first structure determination by molecular replacement, on yellow fin tuna myoglobin.

    • With Wayne Hendrickson he developed a unified way of expressing the phase angle probability density function - it makes use of coefficients A, B, C, D that have come to be a shorthand name for the process. The ABCD curve is still used in most software packages. It is through this representation that each structure factor can be given a proper weight in Fourier syntheses.

    • He also wrote a program that calculated the solution scattering profile I(S) from a set of atomic coordinates many times faster than existing algorithms.

  • Crystallographic Studies of wild type and mutant Staphylococcal nuclease. 
    • At Johns Hopkins there was a large group of researchers that used nuclease as a model system for many purposes. In collaboration with a number of these groups, the Lattman lab undertook a crystallographic and solution studies of nuclease, primarily to study protein folding and electrostatics. An unexpected outcome of this work was the realization that in many cases nuclease can tolerate amino acid substitutions that place ionizable side chains in the hydrophobic core of the protein. Nuclease stabilizes the buried groups by burying water molecules along with them, and also by shifting the pKa of the groups by up to 5 units. This finding stimulated a complete reevaluation about the meaning and value of the dielectric constant within a protein molecule.

Record as HWI CEO. Lattman inherited the CEO post from George DeTitta, under whose leadership HWI had grown and prospered. Lattman’s key goals were to advance the HWI mission of basic research by developing new revenue and support streams to replace the faltering system of federal grants. His key achievements in this area are:

  • A contract with a consortium of six major big pharma companies, the Industrial Macromolecular Crystallography Association or IMCA; manage a large x-ray diffraction facility that IMCA operates at the Argonne National Laboratory.
  • The launch of the startup company HarkerBIO, which is wholly owned by HWI and promises important new revenues to support research at the Institute.
  • The hiring of HWI scientist Michael Malkowski as full professor and Chair of the UB Department of Structural Biology.  This hiring is a first step towards regularizing the status of this Department, which has until now largely been staffed by HWI scientists serving on a volunteer basis.
  • Leadership in a major NSF Science and Technology Center, Biology with X-ray Free Electron Lasers (BioXFEL), that promises to keep HWI at the leading edge of technology and visibility.


700 Ellicott Street Buffalo, New York 14203-1102 Tel: 716 898 8600 Fax: 716 898 8660