Other Info

Hal A. Lewis

Brookhaven National Laboratory
From: 1/5/99- 6/14/00

Past BNL Research Interests

I am the biology beamline scientist at x-ray beamline X25 at the National Synchrotron Light Source and as such am responsible for the operation and development of the research facility for macromolecular crystallography at X-25. This beamline posses a wiggler insertion device making it the brightest among the biology-devoted NSLS x-ray beamlines and so of great value to crystallographers with difficult crystallographic problems.

Also, I'm continuing and expanding a collaboration with Professors R. Darnell and S. Burley at Rockefeller University concerning the function and structure of neuronal RNA-binding proteins bound to their in vivo RNA ligands. This initially will entail solving the co-structure of the Nova protein (discovered at Rockefeller) with its RNA ligand then expand into the study of the FMR-1 protein and its RNA ligand, an important area in the field of hereditary mental retardation. This research will also contribute to our understanding of the various ways proteins use to specifically recognize RNA sequences and structure.

Participation in the BNL/Rockefeller/Albert Einstein Structural Genomics pilot. The goal of this project is to rapidly determine one member of each family of protein folds yet undiscovered as well as to develop the methodology and instrumentation that will speed up the process of x-ray crystallographic structure determination of proteins through the use of automated synchrotron data collection.

Structure of a Nova KH domain. Ribbon diagram of Nova KH3 with conserved aliphatic residues comprising the hydrophobic core illustrated in ball and stick format. The invariant Gly-X-X-Gly is shown in yellow, and the invariable loop in red. (a) a view of the beta-sheet face of the KH domain. (b) A 90 degree rotation from the view in (a).
From H.A. Lewis et al. Structure Fold Des., 7(2):91-203 (1999).

Past Selected Publications

Jensen K.B., Musunuru K., Lewis H.A., Burley S.K. and Darnell R.B.
The tetranucleotide UCAY directs the specific recognition of RNA by the Nova KH3 domain.
Proc Natl Acad Sci U S A., 97(11):5740-5745 (2000). PubMed
Lewis H.A., Musunuru K., Edo C., Jensen K.B., Darnell R.B. and Burley S.K.
Sequence specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome.
Cell, 100(3):323-332 (2000). PubMed
Lewis H.A., Chen H., Edo C., Bukanovich R.J., Yang Y.Y.L., Musunuru K., Zhang R., Darnell R.B. and Burley S.K.
Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains.
Structure Fold Des., 7(2):191-203 (1999). PubMed
Santalucia Jr. J., Shen L.X., Cai Z., Lewis H.A. and Tinoco Jr. I.
Synthesis and NMR of RNA with selective isotropic enrichment in the bases.
Nucl. Acids Res., 23:4913-4921 (1995).
Denton M.B., Lewis H.A. and Sims G.R.
Charge-injection and charge-coupled devices in practical chemical analysis.
in: Multichannel Image Detectors, (Y. Talmi, edt.),
ACS Symposium Series, 236(2): 133-154 (1982).
Lewis H. A. and Denton M.B.
Determination of the ultraviolet and visible spectral response of a charge-injections device array detector.
J. Auto. Chem., 3:9-12 (1981).

Last Modified: April 10, 2009
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