Elsevier

Methods

Volume 1, Issue 1, August 1990, Pages 100-104
Methods

Crystallization of designed protein variants

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Over 300 mutants of bacteriophage T4 lysozyme have been constructed and about 80% of these give crystals suitable for X-ray diffraction analysis. All crystals were obtained under batch conditions similar to those used initially for the wild-type protein. The principal reasons for noncrystallization of some mutants appear to be disruption of crystal contacts and/or conformational changes in the protein. Mutations that do not disrupt crystal contacts and do not cause changes in conformation can be routinely crystallized isomorphously with wild-type lysozyme. Occasionally, a crystal modification non-isomorphous with wild-type is obtained. The structure of one such variant (Met 6 → Ile) has recently been determined and found to display a striking range of conformational states within the same crystal.

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