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Structure of a T=1 aggregate of alfalfa mosaic virus coat protein seen at 4·5 Å resolution
Ist Teil von
Journal of molecular biology, 1983, Vol.167 (4), p.873-890
Ort / Verlag
Elsevier Ltd
Erscheinungsjahr
1983
Link zum Volltext
Quelle
Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)
Beschreibungen/Notizen
A
T=1 empty aggregate of alfalfa mosaic virus coat protein had been crystallized in a hexagonal unit cell and its orientation was determined with the rotation function. A single heavy-atom derivative has now been prepared and the position of the two Hg atoms per protein subunit were determined using a systematic Patterson search procedure, given the particle orientation. Phases, initially determined by single isomorphous replacement, were refined by six cycles of electron density averaging and solvent leveling to produce a 4·5 Å resolution electron density map.
The protein coat is confined between 95 and 58 Å radius. The subunit boundary could be delineated easily. It has a central cavity reminiscent of the
β-barrel in other spherical plant viruses, but its topology could not be determined unambiguously. The spherical particle has large holes at the 5-fold axes, consistent with previous observations. The subunits have substantial interactions at the 2 and 3-fold axes. The structure of the elongated particles is discussed in relation to these results.