The present work investigated the correlation of the molecular order/disorder in crystals of supramacromolecular protein complexes with crystallization processes and conditions. For this purpose, the model protein lumazine synthase from B. subtilis was crystallized under different transport conditions, e.g. under reduced gravity and in the presence of homologous impurities. Electron microscopic investigations of crystal surfaces enabled the visualization, analysis and quantification of crystal defects. The results showed high point defect density (10E9 to 10E10 defects/cm²), which were essentially caused by molecules which adopted "false" orientations in the crystal lattice.
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The present work investigated the correlation of the molecular order/disorder in crystals of supramacromolecular protein complexes with crystallization processes and conditions. For this purpose, the model protein lumazine synthase from B. subtilis was crystallized under different transport conditions, e.g. under reduced gravity and in the presence of homologous impurities. Electron microscopic investigations of crystal surfaces enabled the visualization, analysis and quantification of crystal d...
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