= Florian Brueckner
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<Florian Brueckner> coauthored structural experiments on how <RNA polymerase II> moves along <DNA> during <transcription>. With <Patrick Cramer>, he prepared crystals containing an elongating <enzyme> complex in which states before and after movement could interconvert. Soaking the crystals with <alpha-amanitin> trapped a new arrangement interpreted as a possible intermediate. The resulting <X-ray crystallography> structure was refined at 3.4 angstrom resolution.<Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation by Florian Brueckner and Patrick Cramer>[abstract, preparation and trapped state]{ref}
The entering <DNA> base lay above a displaced <RNA polymerase bridge helix>, while the <RNA polymerase trigger loop> adopted a wedged arrangement. The authors proposed that the inhibitor restricts movement of these parts, interfering with both <nucleotide> incorporation and advancement. This illustrates a productive use of inhibition: slowing a molecular machine can make otherwise transient arrangements accessible to structural measurement. The data support a mechanistic model, rather than providing a direct movie of every motion in a living <biological cell>.<Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation by Florian Brueckner and Patrick Cramer>[abstract, bridge helix, trigger loop and proposed mechanism]{ref}
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