International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F. ch. 5.1, p. 111   | 1 | 2 |

Section 5.1.1.1.2. Quality of protein crystals

H. L. Carrella* and J. P. Gluskera

aThe Institute for Cancer Research, The Fox Chase Cancer Center, Philadelphia, PA 19111, USA
Correspondence e-mail:  hl_carrell@fccc.edu

5.1.1.1.2. Quality of protein crystals

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Protein and nucleic acid crystals contain a high proportion of water in each unit cell and are therefore fragile. The proportion of solvent to macromolecule in the crystal can be expressed, as described by Matthews (1968[link]), as Vm in Å3 Da−1 for the asymmetric unit. Values in the range 1.7 to 4.0 are usual for proteins, but nucleic acid crystals generally have a higher water content. Crystal fragility due to water content may be used to determine whether or not a crystal contains protein or buffer salt. Pressure with a fine probe will settle this question because a protein crystal will shatter, while a salt crystal, which is much sturdier, will generally withstand such treatment. If crystals have grown into one another, or appear as clumps, it is sometimes possible to split off a single crystal by prodding the clump gently at the junction point between the crystals with a scalpel or a glass fibre.

References

First citation Matthews, B. W. (1968). Solvent content in protein crystals. J. Mol. Biol. 33, 491–497.Google Scholar








































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