Crystallization of the N-terminal domain of DFF45: the mutual chaperone mechanism is challenged
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Updated: Jul 27, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
1Laboratory of Structural Biology, School of Life Sciences and Engineering Tsinghua University, Beijing 100084, China.
Abstract:
DNA fragmentation factor 45 (DFF45) regulates DNase DFF40 as its inhibitor and chaperone. It was reported that the N-terminal domain (NTD) of DFF45 alone is disordered and DFF40 is necessary as a mutual chaperone for the folding of NTD. However, here we reported the crystallization of DFF45 NTD. These crystals diffract to 9A using a synchrotron radiation source. In spite of the low resolution, the demonstration of crystal formation indicates that DFF45 NTD itself is not unstructured, which strongly questions the mutual chaperone speculation about DFF45 and DFF40.
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