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PDBsum entry 6d5r
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References listed in PDB file
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Key reference
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Title
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The impact of cryosolution thermal contraction on proteins and protein crystals: volumes, Conformation and order.
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Authors
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D.H.Juers,
C.A.Farley,
C.P.Saxby,
R.A.Cotter,
J.K.B.Cahn,
R.C.Holton-Burke,
K.Harrison,
Z.Wu.
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Ref.
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Acta Crystallogr D Struct Biol, 2018,
74,
922-938.
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PubMed id
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Abstract
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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.
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