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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DNA Transactions at an Atomic Level
The genetic information encoded within DNA is copied, maintained, and decoded by protein machines. Our laboratory uses electron microscopy, X-ray crystallography, and other high-resolution structural and biochemical approaches to investigate the molecular details of how these proteins repair damaged DNA and maintain integrity of the genome during replication.
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Cool story on Noah and Katie's 2022 mBio publication
Professor Eichman elected as AAAS Fellow
Noah receives the 2022 Edward Ferguson Jr. Graduate Award from the Graduate School
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