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

Emerging roles of DNA glycosylases and the base excision repair pathway. Trends Biochem Sci

In the News

Katherine Amidon receives Honorable Mention for NSF fellowship

Professor Eichman honored with endowed chair

Former PhD student Sonja Brooks Fulmer featured on Beyond the Lab

Alyssa and Noah awarded 3-year NSF Graduate Research Fellowships

News Archives

Training Opportunities Available

  • 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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  • Structural studies of the vertebrate replisome
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  • E. coli AidB is a DNA binding protein involved in the bacterial adaptive response to alkylating agents
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