Using x-ray vision, he keeps his eye on the bacteria

"Dr. C. Erec Stebbins, head of Rockefeller University's Laboratory of Structural Microbiology, spends much of his time using a nearly 100-year-old investigative tool..."

-The New York Times


Threading a narrow needle

"A high-resolution crystal structure obtained by Jorge E. Galán, a microbiologist at Yale..."

-Chemical & Engineering News


Rockefeller researchers solve structure for deadly bacterial toxin

"Researchers at Rockefeller University, New York, have determined the structure of a potent DNA-damaging protein..."

-Drug Discovery & Development


A salmonella invasion protein that acts as a "molecular staple"

"Salmonella invasion protein A (SipA) is an important virulence factor injected into host cells, where it modulates the cytoskeleton by polym-erizing actin..."

-Science

Graduate School Publications


1:


C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, and N.P. Pavletich. (1997). "Crystal Structure of an Hsp90-Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent." Cell 89, 239-250.
[Abstract]  [pdf]





2:


C.E. Stebbins, W.G. Kaelin, and N.P. Pavletich. (1999). "Structure of the VHL-ElonginC-ElonginB complex: implications for von Hippel-Lindau tumor suppressor function." Science, 284, 455-461.
[Abstract]  [pdf]





3:


M. Ohh, Y. Takagi, T. Aso, C.E. Stebbins, N. P. Pavletich, B. Zbar, R. C. Conaway, J. W. Conaway, and W. G. Kalin, Jr. (1999). "Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein." J. Clin. Invest. 104, 1583-1591.
[Abstract]  [pdf]