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

1.在N端与SlyD融合的管状启动子蛋白gp48以可溶部分形式表达并结晶。2.从噬菌体PP01中分离出与gp38共同构成尾部纤维的gp37的C-末端结构域，并分离和结晶了化学计量比为3：1的复合体。结果表明，C末端的13 kDa多肽是自切的。3.成功地将Holin的可溶性结构域与快速裂解蛋白GP-Ri的复合体结晶并确定了其结构，为进一步了解其裂解抑制机制奠定了基础。

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.