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The effect of relative humidity (rH) on protein crystal structures, an area that has attracted high scientific interest during the past decade, is investigated in this study on hen egg-white lysozyme (HEWL) polycrystalline precipitates via in situ laboratory X-ray powder diffraction (XRPD) measurements. For this purpose, HEWL was crystallized at room temperature and pH 4.5, leading to a novel monoclinic HEWL phase which, to our knowledge, has not been reported before. Analysis of XRPD data collected upon rH variation revealed several structural modifications. These observations, on a well-studied molecule like HEWL, underline not only the high impact of humidity levels on biological crystal structures, but also the significance of in-house XRPD as an analytical tool in industrial drug development and its potential to provide information for enhancing manufacturing of pharmaceuticals.

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Portable Document Format (PDF) file https://doi.org/10.1107/S1600576718013936/ap5031sup1.pdf
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Text file https://doi.org/10.1107/S1600576718013936/ap5031sup2.txt
Synchrotron powder diffraction data of hen-egg white lysozyme crystallized at pH 4.5 (293K), in monoclinic symmetry. Data were collected at ESRF \[ID22, λ=0.79988(5) Å, room temperature\]


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