Elsevier

Analytical Biochemistry

Volume 168, Issue 1, January 1988, Pages 141-147
Analytical Biochemistry

A simple apparatus for controlling nucleation and size in protein crystal growth

https://doi.org/10.1016/0003-2697(88)90021-8Get rights and content

Abstract

A simple device is described for controlling vapor equilibrium in macromolecular crystallization as applied to the protein crystal growth technique commonly referred to as the “hanging drop” method. Crystal growth experiments with hen egg white lysozyme have demonstrated control of the nucleation rate. Nucleation rate and final crystal size have been found to be highly dependent upon the rate at which critical supersaturation is approached. Slower approaches show a marked decrease in the nucleation rate and an increase in crystal size.

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    Citation Excerpt :

    Experimental studies of protein crystallisation have focused on obtaining high quality large crystals in order to perform X-ray diffraction analysis with the aim of obtaining the 3-dimensional structure of protein molecules. The experiments [1–11] often used micro-volume protein solutions and were carried out by changing concentration via evaporation. Typical equipment involves high-throughput micro-crystallisers, in which a large number of experiments are conducted and repeated, sometimes by applying external fields such as electric, magnetic, electromagnetic, and micro-gravity [12].

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1

K.M.G. was supported by the Universities Space Research Association.

2

Tennessee Scientific Glass Co., Fayetteville, TN.

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