Crystallization of mutant lysozymes from bacteriophage T4
The crystallization properties of a large number of T4 lysozyme mutant proteins have been analyzed. Approximately 80% of the mutant proteins crystallize under conditions very similar to those used for the wild-type protein, regardless of the type of amino acid substitution or its location. Of the mutants that crystallize all but two, A146F (tetragonal) and M6I (orthorhombic), are isomorphous with wild-type lysozyme (trigonal). The two nonisomorphous crystals are obtained in cases where internal residues are changed. Substitution of a large side chain for a small one, as in A146F, appears to exceed a critical internal packing volume above which nonisomorphism is induced. The nonisomorphism of M6I may be due to structural changes induced by the introduction of a β-branched side chain. © 1988.
Brennan, RG; Wozniak, J; Faber, R; Matthews, BW
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