High-pressure macromolecular crystallography as a tool for studying protein flexibility

Lieske, J.; Saouane, S.; Reinke, P.Y.A.; Falke, S.; Ewert, W.; Meyer, J.; Pakendorf, T.; Burkhardt, A.; Crosas, E.; Hakanpää, J.; Stachnik, K.; Sieg, J.; Rarey, M.; Aßmann, M.; Zaun, H.; Kuballa, J.; Selikhanov, G.K.; Gabdulkhakov, A.G.; Chapman, H.N.; Günther, S.; Meents, A.

doi:10.1107/S2052252526008468

Figure 2
Changes in (a) unit-cell volumes and (b) void volumes of the five studied proteins at different pressures. All values are normalized to the corresponding values at atmospheric pressure. The depicted unit-cell volumes are the normalized average volumes calculated from 2–19 individual crystals, with the error bars displaying the normalized mean of the estimated standard deviation of the unit-cell volume. Void volumes were calculated from the refined structures using ProteinVolume 1.3 (Chen & Makhatadze, 2015

). Due to the incompleteness of the data sets, there are no void volume values for M^pro and AGE after pressure release.

IUCrJ

Volume 13| Part 6| November 2026|

ISSN: 2052-2525

https://doi.org/10.1107/S2052252526008468

BIOLOGY | MEDICINE

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