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@ARTICLE{Klsch:884043,
      author       = {Kölsch, A. and Radon, C. and Golub, M. and Baumert, A. and
                      Bürger, J. and Mielke, T. and Lisdat, F. and Feoktystov, A.
                      and Pieper, J. and Zouni, A. and Wendler, P.},
      title        = {{C}urrent limits of structural biology: the transient
                      interaction between cytochrome c and photosystem {I}},
      journal      = {Current research in structural biology},
      volume       = {2},
      issn         = {2665-928X},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2020-03063},
      pages        = {171-179},
      year         = {2020},
      abstract     = {Trimeric photosystem I from the cyanobacterium
                      Thermosynechococcus elongatus (TePSI) is an intrinsic
                      membrane protein, which converts solar energy into
                      electrical energy by oxidizing the soluble redox mediator
                      cytochrome c6 (Cyt c6) and reducing ferredoxin. Here, we use
                      cryo-electron microscopy and small angle neutron scattering
                      (SANS) to characterize the transient binding of Cyt c6 to
                      TePSI. The structure of TePSI cross-linked to Cyt c6 was
                      solved at a resolution of 2.9 Å and shows additional
                      cofactors as well as side chain density for $84\%$ of the
                      peptide chain of subunit PsaK, revealing a hydrophobic,
                      membrane intrinsic loop that enables binding of associated
                      proteins. Due to the poor binding specificity, Cyt c6 could
                      not be localized with certainty in our cryo-EM analysis.
                      SANS measurements confirm that Cyt c6 does not bind to TePSI
                      at protein concentrations comparable to those for
                      cross-linking. However, SANS data indicate a complex
                      formation between TePSI and the non-native mitochondrial
                      cytochrome from horse heart (Cyt cHH). Our study pinpoints
                      the difficulty of identifying very small binding partners
                      (less than $5\%$ of the overall size) in EM structures when
                      binding affinities are poor. We relate our results to well
                      resolved co-structures with known binding affinities and
                      recommend confirmatory methods for complexes with KM values
                      higher than 20 μM.},
      cin          = {JCNS-FRM-II / JCNS-2 / MLZ},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-2-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS1-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000658373100016},
      pubmed       = {34235477},
      doi          = {10.1016/j.crstbi.2020.08.003},
      url          = {https://juser.fz-juelich.de/record/884043},
}