Rational ‘correction’ of the amino-acid sequence of RbcX protein from the thermophilic cyanobacterium Thermosynechococcus elongatus dramatically improves crystallization
AUTOR(ES)
Tarnawski, Miroslaw
FONTE
International Union of Crystallography
RESUMO
Recombinant RuBisCO chaperone from T. elongatus, TeRbcX, was aggregated and could not be crystallized. Mutations of an unusual Cys residue in the TeRbcX sequence yielded much better behaved proteins that could rapidly be crystallized.
