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The level of structural detail around the metal sites in Ni2+ and Cu2+ T6 insulin derivatives was significantly improved by using a combination of single-crystal X-ray crystallography and X-ray absorption spectroscopy. Photoreduction and subsequent radiation damage of the Cu2+ sites in Cu insulin was followed by XANES spectroscopy.

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A combination of powder diffraction and macromolecular crystallography demonstrated the presence of at least three different crystal forms of B. lentus subtilisin in a suspension from a large-scale industrial production. The application of powder diffraction is a powerful tool for quality control in enzyme production.
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