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

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

• Crystallographic studies of stability and function mutants of staphylococcal nuclease
• Protein electrostatics
• Protein folding
• Development and improvement of methods in protein crystallography
• Drug Design

During his career Eaton Lattman has worked on number of major research themes,  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 atomic coordinates many times faster that 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.
  • Interests as HWI CEO. Under the leadership of George DeTitta HWI has grown and prospered. It is Lattman's hope to maintain and promote the upward trajectory of the Institute. His primary goals are to advance and diversify both the research and educational enterprises of HWI. A key need is to add new faculty members who will broaden the research base of the Institute, and connect it more closely to sister institutions in the BNMC and elsewhere. Faculty will be involved in all stages of hiring and recruitment, from helping to choose the research area to evaluating the candidates. In parallel with the need for new faculty is the need to promote the programs of current faculty. This will come about by working with faculty and staff to identify or help forward new research opportunities. Such opportunities would include developing new collaborations, and identifying new sources of funding from federal or other agencies. 
A final key element is to continue to promote the State's Biotechnology initiative in western New York.  By working with other units to develop cluster hires and other initiatives we can leverage the basic research orientation of HWI into an engine that that will promote growth at large.
700 Ellicott Street Buffalo, New York 14203-1102 Tel: 716 898 8600 Fax: 716 898 8660