DNA Transactions at an Atomic Level

The genetic information encoded within DNA is copied, maintained, and decoded by protein machines. Our laboratory uses X-ray crystallography and other high-resolution structural and biochemical approaches to investigate the molecular details of how these proteins repair damaged DNA and carry out DNA synthesis.

Featured Article

An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3. J Biol Chem


In the News

Katherine awarded NIH F31 pre-doctoral fellowship

Katherine named 2020 Vanderbilt Prize Student Scholar

New NIH grant to study the DNA replication-repair interface

Noah's NAR paper selected as a Breakthrough Article and landed the cover

Professor Eichman honored with the 2021 International Award from the Biochemical Society


News Archives


Training Opportunities Available


  • High-resolution structure of a native DNA-protein crosslink
     
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  • Time-resolved crystallography to monitor base excision repair by DNA glycosylases
     
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  • HLTF's ancient HIRAN domain binds 3' DNA ends to drive replication fork reversal
     
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  • Bacterial AlkD is the first glycosylase discovered to repair a bulky lesions like the natural product yatakemycin
     
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  • How do DNA repair enzymes search the genome for chemical damage?

  • How are stalled replication forks repaired?

  • SMARCAL1 HARP domain is important for reversal of stalled forks
     
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  • HEAT repeats have emerged as an important nucleic acid binding architecture

  • Base flipping is not a prerequisite for excision repair by DNA glycosylases
     
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  • CH-π interactions important for catalysis of base excision by DNA glycosylase AlkD
     
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  • Crystals used to determine the atomic structures of a protein-DNA complex

  • X-ray diffraction image from a protein crystal

  • Building the atomic structure of a protein-DNA complex into experimental electron density from X-ray diffraction data

  • NMR chemical shift perturbation to monitor protein structural changes induced by DNA binding
     
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