Preliminary studies on the denaturation of cross-linked lysozyme crystals.
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.
D001966:Bromine; D002712:Chlorides; D003461:Crystallography; D000431:Ethanol; D006146:Guanidines; D008094:Lithium; D009113:Muramidase; D011489:Protein Denaturation; D014508:Urea; D014961:X-Ray Diffraction
D002712:Chlorides; D006146:Guanidines; D000431:Ethanol; D014508:Urea; D008094:Lithium; D009113:Muramidase; D001966:Bromine