= Patrick Cramer
{c}
<Patrick Cramer> studies the molecular machinery of <transcription>: how <RNA polymerases> copy information from <DNA> into <RNA>. His work connects the three-dimensional structures of these <enzymes> with the steps by which they add <nucleotides> and advance along a template. https://www.mpg.de/president[Institutional research description, Gene transcription]{ref}
With <Florian Brueckner>, Cramer used <alpha-amanitin> to trap a possible intermediate in the movement of <RNA polymerase II>. A structure at 3.4 angstrom resolution showed a shifted <RNA polymerase bridge helix> and a particular position of the <RNA polymerase trigger loop>.<Structural basis of transcription inhibition by alpha-amanitin and implications for RNA polymerase II translocation by Florian Brueckner and Patrick Cramer>[abstract, inhibitor-soaked crystals and structural interpretation]{ref}
A useful way to understand this strategy is to distinguish an <enzyme>'s chemical reaction from its mechanical reset: after extending an <RNA> chain, the machinery must position the next template base. Trapping different arrangements can reveal how those tasks are coordinated. A trapped structure is a snapshot under experimental conditions, however, so assigning it to the normal reaction cycle also requires biochemical evidence.
\Image[https://www.mpg.de/11655279/original-1646387574.jpg]
{title=Patrick Cramer}
{description=Portrait identified on https://www.mpg.de/7894444/multidisciplinary-sciences-cramer[his Max Planck Society profile].}
{height=300}
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