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Updated: Jul 22, 2026

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Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Preliminary studies on the denaturation of cross-linked lysozyme crystals
Biophysical Journal
|May 1, 1968
Abstract:
When monoclinic lysozyme crystals are fully cross-linked with glutaraldehyde, and then the protein molecules are denatured while in the crystalline state, a single crystal-gel is formed which is a jelly-like crystal of a denatured protein molecule. It is highly disordered, but has crystalline optical and morphological properties and can be renatured to a cross-linked crystal resembling the original crystal as determined from the X-ray diffraction pattern. Experiments with the following denaturants are described: guanidinium chloride, bromoethanol, urea, and lithium chloride.

