Abstract
The structural protein, gene product 9 (gp9), of bacteriophage T4 controls baseplate expansion at the first steps of virus attachment onto its host bacterial cell with subsequent tail contraction. Gp9, which has an M r of 30·8 kDa and contains 287 amino acids, has been purified from a recombinant Escherichia coli strain and crystallized at 25°C using the hanging drop vapor diffusion method at pH 4·0 with ammonium sulfate as precipitant. The crystals of gp9 belong to the space group R 32 with hexagonal cell dimensions a= b=86·5 Å and c = 156·2 Å and diffract X-rays to at least 2·7 Å. There is one molecule per asymmetric unit.
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