Arnd B. E. Brauer
Free University of Berlin
8 Papers
40 Citations
Arnd B. E. Brauer is an academic researcher from Free University of Berlin. The author has contributed to research in topics: Transfer RNA & Aminoacylation. The author has an hindex of 5, co-authored 8 publications.
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Papers
Crystal structure of an Escherichia coli tRNAGly microhelix at 2.0 Å resolution
Charlotte Förster,Arnd B. E. Brauer,M. Perbandt,Daniel Lehmann,J.P. Fürste,Ch. Betzel,Volker A. Erdmann +6 more
TL;DR: The crystal structure of an Escherichia coli tRNA Gly aminoacyl stem microhelix at 2.0 A resolution is presented and the helical parameters, solvent molecules and a potential magnesium binding site are discussed.
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Comparative crystallization and preliminary X-ray diffraction studies of locked nucleic acid and RNA stems of a tenascin C-binding aptamer.
Charlotte Förster,Arnd B. E. Brauer,Svenja Brode,Kathrin Schmidt,Markus Perbandt,Arne Meyer,Wojciech Rypniewski,Christian Betzel,Jens Kurreck,Jens P. Fürste,Volker A. Erdmann +10 more
TL;DR: Here, the crystallographic and X-ray diffraction data of the isolated aptamer stem encompassed in a six-base-pair duplex both with and without the LNA modification are presented.
tRNASer acceptor stem: conformation and hydration of a microhelix in a crystal structure at 1.8 Å resolution
Charlotte Förster,Arnd B. E. Brauer,Svenja Brode,Jens P. Fürste,Christian Betzel,Volker A. Erdmann +5 more
TL;DR: The crystal structure of a serine-specific tRNA acceptor-stem microhelix, the binding site for the seryl-tRNA synthetase, was solved by X-ray analysis and the role of the specific hydration pattern and of the irregular conformation of the tRNA(Ser) acceptor -stem helix is discussed and summarized.
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Human tRNAGly acceptor‐stem microhelix: crystallization and preliminary X‐ray diffraction analysis at 1.2 Å resolution
Charlotte Förster,Karol Szkaradkiewicz,Markus Perbandt,Arnd B. E. Brauer,Tordis Borowski,Jens P. Fürste,Christian Betzel,Volker A. Erdmann +7 more
TL;DR: The human tRNA(Gly) acceptor-stem microhelix was crystallized in an attempt to analyze the structural features that govern the correct recognition of tRNAs by the eukaryotic/archaebacterial-type glycyl-tRNA synthetase.
Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNAGly acceptor-stem microhelix
Charlotte Förster,Markus Perbandt,Arnd B. E. Brauer,Svenja Brode,Jens P. Fürste,Christian Betzel,Volker A. Erdmann +6 more
TL;DR: To obtain further insight concerning structural investigation of the identity elements of the tRNA identity elements, the Escherichia coli seven-base-pair tRNA(Gly) acceptor-stem helix was crystallized.