Appropriate treatment of X-ray diffraction from an unoriented 18-heavy atom
cluster derivative of a yeast RNA polymerase II crystal gave significant p
hase information to 5 Angstrom resolution. The validity of the phases was s
hown by close similarity of a 6 Angstrom electron density map to a 16 Angst
rom molecular envelope of the polymerase from electron crystallography. Com
parison of the 6 Angstrom X-ray map with results of electron crystallograph
y of a paused transcription elongation complex suggests functional roles fo
r 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 tra
nscript from about 8-18 residues upstream of the 3'-end in a tunnel.