Structure and assembly of the central hub of the baseplate of bacteriophage T4

1.在可溶性级分中表达在N-末端与SlyD融合的管起始蛋白gp 48并结晶。2.将来自噬菌体PP 01的gp 37的C-末端结构域与gp 38共同表达，并分离和结晶具有3：1化学计量比的复合物。结果表明，C-末端13 kDa多肽是自切割的。3.将holin的可溶性结构域与快速裂解蛋白gp rI的复合物结晶，并成功地确定了其结构，这将有助于理解裂解抑制机制。

1. Tube initiator protein, gp48, which were fused with SlyD at the N-terminus was expressed in a soluble fraction and crystallized. 2. The C-terminal domain of gp37 from phage PP01 which constitutes the tail fiber together with gp38 were co-expressed and the complex with 3:1 stoichiometry was isolated and crystallized. It was shown that the C-terminal 13 kDa polypeptide was self-cleaved. 3. The complex of the soluble domain of the holin and the rapid lysis protein gp rI was crystallized and the structure has been successfully determined, which is expected to contribute to understanding the mechanisma of lysis inhibition.