General objectives are the use of x-ray crystallography to determine the three-dimensional structures of proteins and the interpretation of those structures. The specific projects are as follows: Completion of the native structure of bovine Cu, Zn superoxide dismutase, including some further cycles of refinement, fitting by computer graphics, and comparison of the four crystallographically-independent subunits. Solution of heavy-atom derivatives and processing of screened-precesion film data in order to obtain first a low-resolution and later a high-resolution structure of the human liver Mn superoxide dismutase (space group P6122, a equals 242A, c equals 81.3A, one dimer per asymmetric unit). Collection of slow-rotation film data, heavy-atom derivative search, and proceeding toward a structure of chicken liver sulfite oxidase (space group R3, a equals 158.2A, c equals 138.3A, one dimer per asymmetric unit). Determining the structure of the Root-effect hemoglobin from spot, starting with phases from our current rotation function results. Search for further generalizations about protein structure, including the use of those generalizations in interpreting low-resolution x-ray data, and the modification of our schematic drawings to serve specific research and teaching needs.
| Richardson, Jane S; Richardson, David C (2014) Biophysical highlights from 54 years of macromolecular crystallography. Biophys J 106:510-25 |
| Richardson, Jane S; Richardson, David C (2013) Studying and polishing the PDB's macromolecules. Biopolymers 99:170-82 |
| Richardson, Jane S; Richardson, David C (2013) Doing molecular biophysics: finding, naming, and picturing signal within complexity. Annu Rev Biophys 42:1-28 |
| Wales, Thomas E; Richardson, Jane S; Fitzgerald, Michael C (2004) Facile chemical synthesis and equilibrium unfolding properties of CopG. Protein Sci 13:1918-26 |
