title: A disulfide polymerized protein crystal.
abstract: 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.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Scheeles väg 2, SE-171 77 Stockholm, Sweden.
authors.forename: Esben M
authors.initials: EM
authors.lastname: Quistgaard
mesh_terms: D003460:Crystallization; D004220:Disulfides / Q000737:chemistry*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry*; D058105:Polymerization; D017434:Protein Structure, Tertiary
chemical_list: C486244:BCAP29 protein, human; D004220:Disulfides; D008565:Membrane Proteins