Crystallization of mutant lysozymes from bacteriophage T4


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Brennan, RG; Wozniak, J; Faber, R; Matthews, BW

Published Date

  • July 2, 1988

Published In

Volume / Issue

  • 90 / 1-3

Start / End Page

  • 160 - 167

International Standard Serial Number (ISSN)

  • 0022-0248

Digital Object Identifier (DOI)

  • 10.1016/0022-0248(88)90311-9

Citation Source

  • Scopus