Autor: |
Roger D. Kornberg, Richard R. Burgess, Grant J. Jensen, Peter R. David, Nancy E. Thompson, Jianhua Fu, David A. Bushnell, Averell Gnatt |
Rok vydání: |
1999 |
Předmět: |
|
Zdroj: |
Cell. 98:799-810 |
ISSN: |
0092-8674 |
DOI: |
10.1016/s0092-8674(00)81514-7 |
Popis: |
Appropriate treatment of X-ray diffraction from an unoriented 18-heavy atom cluster derivative of a yeast RNA polymerase II crystal gave significant phase information to 5 Å resolution. The validity of the phases was shown by close similarity of a 6 Å electron density map to a 16 Å molecular envelope of the polymerase from electron crystallography. Comparison of the 6 Å X-ray map with results of electron crystallography of a paused transcription elongation complex suggests functional roles for two mobile protein domains: the tip of a flexible arm forms a downstream DNA clamp; and a hinged domain may serve as an RNA clamp, enclosing the transcript from about 8–18 residues upstream of the 3′-end in a tunnel. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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