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.
journal_name
Protein Pept Lettjournal_title
Protein and peptide lettersauthors
Li T,Li X,Yang W,Rao Z,Zhai Zhdoi
10.2174/0929866033479068subject
Has Abstractpub_date
2003-04-01 00:00:00pages
221-5issue
2eissn
0929-8665issn
1875-5305journal_volume
10pub_type
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