Acta Crystallographica Section D
b = 84.97, c = 202 A , = 90.36, = 92.97, = 109.94 . An unambiguous molecularreplacement solution was found using the C-terminal portion of the T7 RNA polymerase structure from the early initiation complex as a search model. Model building and structure renement are now in progress. Received 29 July 2002 Accepted 29 October 2002 1. Introduction Although the DNA-dependent RNA polymerase (RNAP) encoded by bacteriophage T7 consists of a single subunit (883 amino acids, 99 kDa), this enzyme is able to carry out all the steps of the transcription cycle in the same manner as the multisubunit RNAPs found in bacteria and eukaryotic cells (McAllister, 1997). The C-terminal portion of phage RNAP (residues 267883, which contains the active site) is structurally related to the pol I-like DNA polymerases and it has been suggested that the N-terminal domain of the phage RNAP confers upon the catalytic core the ability to carry out the steps that are specic to the transcription proc
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