Abstract
Sequence-register shifts remain one of the most elusive errors in experimental macromolecular models. They may affect model interpretation and propagate to newly built models from older structures. In a recent publication, it was shown that register shifts in cryo-EM models of proteins can be detected using a systematic reassignment of short model fragments to the target sequence. Here, it is shown that the same approach can be used to detect register shifts in crystal structure models using standard, model-bias-corrected electron-density maps (2mF
o − DF
c). Five register-shift errors in models deposited in the PDB detected using this method are described in detail.
Publisher
International Union of Crystallography (IUCr)
Cited by
1 articles.
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