The use of low-resolution phasing followed by phase extension from 7.6 to 2.5 A resolution with noncrystallographic symmetry to solve the structure of a bacteriophage capsid protein.
P2, the major capsid protein of bacteriophage PM2, adopts the double β-barrel fold characteristic of the PRD1-adenoviral lineage. The 2.5 Å resolution X-ray data obtained by analysis of the two major lattices of a multiple crystal of P2 were phased by molecular replacement, using as a search model s...
| Main Authors: | , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2011
|