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![[Figure 3]](tz5104fig3mag.jpg)
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Figure 3
Example protein Bragg peak-subtracted, azimuthally averaged diffraction patterns from apoferritin, thaumatin and lysozyme crystals for which ice formed in internal crystal solvent. Crystals were either used as-grown (0%) or were soaked in solutions containing 20% glycerol and cooled to 220 K (top) or 100 K (bottom). The insets show the corresponding 2D diffraction patterns. Largely hexagonal ice diffraction from as-grown lysozyme crystals (which have narrow solvent cavities and little bulk-like solvent) cooled to 100 K arises from ice within solvent pockets that form inside the crystal to accommodate solvent squeezed out by the contracting protein lattice. |
![[Figure 3]](tz5104fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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