Abstract
We report here a series of studies on the controlled contamination of crystallizing solutions of the hexagonal form of turkey egg white lysozyme (TEWL) carried out to understand the effects of impurities on the nucleation and growth of protein crystals. The contamination of TEWL solutions with any of three other avian lysozymes affects both the nucleation and the growth processes. For hen and quail egg white lysozymes, low and medium levels of contamination result in partial inhibition of nucleation and shortening of the c-axis. Further increase of the contaminant concentration leads to detectable co-crystallization. A different effect is obtained when using the pheasant egg white lysozyme. Contamination by an unrelated protein, ribonuclease A, has an effect on the nucleation levels that is similar to those observed with the avian lysozymes. However, no effect on TEWL crystal morphology is observed. Thus, in the case of TEWL crystals, one can distinguish between a specific effect on crystal morphology induced by related proteins and a more general inhibitory effect on the nucleation levels observed in all cases studied here.
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