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Esben Meldgaard Høgh Quistgaard

A disulfide polymerized protein crystal

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The vDED coiled coil domain from human BAP29 was crystallized in dimeric and tetrameric forms. For the dimer, a disulfide bond was unexpectedly found to bridge a crystal contact, resulting in complete cross-linking along the c-axis. This indicates that it is in principle possible to design spontaneously polymerizing protein crystals.

Original languageEnglish
JournalChemical Communications
Volume50
Issue95
Pages (from-to)14995-14997
Number of pages3
ISSN1359-7345
DOIs
Publication statusPublished - 2014
Externally publishedYes

    Research areas

  • DESIGN, RESIDUES, SYMMETRY, POROSITY, COMPLEX, ARRAYS

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