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@ARTICLE{Hentschel:904360,
      author       = {Hentschel, Lorena and Hansen, Jan and Egelhaaf, Stefan U.
                      and Platten, Florian},
      title        = {{T}he crystallization enthalpy and entropy of protein
                      solutions: microcalorimetry, van't {H}off determination and
                      linearized {P}oisson–{B}oltzmann model of tetragonal
                      lysozyme crystals},
      journal      = {Physical chemistry, chemical physics},
      volume       = {23},
      number       = {4},
      issn         = {1463-9076},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2021-05930},
      pages        = {2686 - 2696},
      year         = {2021},
      abstract     = {During a first-order phase transition, a thermodynamic
                      system releases or absorbs latent heat. Despite their
                      fundamental importance, the heat or enthalpy change
                      occurring during protein crystallization has been directly
                      measured only in a few cases, and the associated entropy
                      change can only be determined indirectly. This work provides
                      an experimental determination and theoretical analysis of
                      the dependence of the molar crystallization enthalpy of
                      lysozyme solutions, ΔHxtal, on the physicochemical solution
                      parameters. Its value is determined directly by isothermal
                      microcalorimetry and indirectly by a van't Hoff analysis of
                      solubility data, which quantitatively agree. This suggests a
                      two-state crystallization process, in which oligomeric
                      intermediates play a minor role. ΔHxtal is found to be
                      negative on the order of few tens of the thermal energy per
                      molecule. It is independent of protein concentration and
                      stirring speed, but weakly depends on salt (NaCl)
                      concentration and solution pH. Assuming that crystals are
                      electrostatically neutral, these trends are explained by a
                      linearized Poisson–Boltzmann theory. In addition, the
                      molar crystallization entropy, ΔSxtal, is analyzed. The
                      dependence of the van't Hoff entropy on salt concentration
                      and pH is captured by the model, complementing the analysis
                      of crystallization thermodynamics.},
      cin          = {IBI-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-4-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33481978},
      UT           = {WOS:000614634000016},
      doi          = {10.1039/D0CP06113A},
      url          = {https://juser.fz-juelich.de/record/904360},
}