6b6o Citations

The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order.

OpenAccess logo Acta Crystallogr D Struct Biol 74 922-938 (2018)

Abstract

Cryocooling of macromolecular crystals is commonly employed to limit radiation damage during X-ray diffraction data collection. However, cooling itself affects macromolecular conformation and often damages crystals via poorly understood processes. Here, the effects of cryosolution thermal contraction on macromolecular conformation and crystal order in crystals ranging from 32 to 67% solvent content are systematically investigated. It is found that the solution thermal contraction affects macromolecule configurations and volumes, unit-cell volumes, crystal packing and crystal order. The effects occur through not only thermal contraction, but also pressure caused by the mismatched contraction of cryosolvent and pores. Higher solvent-content crystals are more affected. In some cases the solvent contraction can be adjusted to reduce mosaicity and increase the strength of diffraction. Ice formation in some crystals is found to cause damage via a reduction in unit-cell volume, which is interpreted through solvent transport out of unit cells during cooling. The results point to more deductive approaches to cryoprotection optimization by adjusting the cryosolution composition to reduce thermal contraction-induced stresses in the crystal with cooling.

Articles - 6b6o mentioned but not cited (1)

  1. The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, conformation and order. Juers DH, Farley CA, Saxby CP, Cotter RA, Cahn JKB, Holton-Burke RC, Harrison K, Wu Z. Acta Crystallogr D Struct Biol 74 922-938 (2018)


Articles citing this publication (3)

  1. The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting. Wright ND, Collins P, Koekemoer L, Krojer T, Talon R, Nelson E, Ye M, Nowak R, Newman J, Ng JT, Mitrovich N, Wiggers H, von Delft F. Acta Crystallogr D Struct Biol 77 62-74 (2021)
  2. Solvent flows, conformation changes and lattice reordering in a cold protein crystal. Moreau DW, Atakisi H, Thorne RE. Acta Crystallogr D Struct Biol 75 980-994 (2019)
  3. Challenges in solving structures from radiation-damaged tomograms of protein nanocrystals assessed by simulation. Peck A, Yao Q, Brewster AS, Zwart PH, Heumann JM, Sauter NK, Jensen GJ. Acta Crystallogr D Struct Biol 77 572-586 (2021)