Abstract
The crystals of most proteins are poorly ordered and diffract to lower resolutions than other crystals of simple and inorganic compounds. The use of two novel methods for gel protein crystal growth, utilizing liquid diffusion and vapor diffusion, are described for the growth of lysozyme and canavalin. Crystallization using gels has been demonstrated to improve crystal quality by reducing convective flow, sedimentation, nucleation and twinning. Preliminary X-ray diffraction data are also presented.

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