Abstract
The sub-atomic structure of the tail-lysozyme complex of bacteriophage T4 has been determined to the resolution of 2.9 Å. For the phase determination, MAD (mufti-wavelength anomalous dispersion) from seleno-methionine-substituted gp27 which had been complexed with unlabeled gp5 (gp = gene product) was utilized. The tail-lysozyme was then localized in the low-resolution structure of the tail baseplate, which revealed the role of the C-terminal β-helix domain as a cell-puncturing device as well as an intra-molecular chaperone to form the trimeric tail-lysozyme complex.
