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 4
C_α—C_α DDMs showing the pressure-induced compression of the structures. Shown are (a) RNaseA at 120 MPa, (b) DRAK2 at 110 MPa, (c) AGE at 80 MPa and (d) the RC at 120 MPa compared with the corresponding structures at atmospheric pressure. Domains are labeled for a better overview. Negative values indicate compression. Maximum compression values differ between protein systems. Maximum values for each system were used for individual color scale definition for clarity. Crystal contacts of the HP structures are indicated as green line patterns below the matrices. Indicated are all interfacing crystallography-related residues according to PISA (Krissinel & Henrick, 2007

IUCrJ

Volume 13| Part 6| November 2026|

ISSN: 2052-2525

https://doi.org/10.1107/S2052252526008468

BIOLOGY | MEDICINE

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