Preparation of a crystallizable mRNA-binding fragment of Moorella thermoacetica elongation factor SelB

A C-terminal 30 kDa fragment of the selenocysteine-specific elongation factor SelB from M. thermoacetica has been recloned, expressed in E. coli and crystallized in a suitable form for X-ray analysis. The crystals diffract to 2.7 Å in an in-house X-ray source.

Parallel cloning, expression, purification and crystallization of human proteins for structural genomics

Insights are gained into high-throughput target selection, cloning, expression and crystallization of human genomic proteins. For example, there was a marked difference seen bewteen the ease of expression of proteins of molecular weight (MW) < 25 kDa (93% success), compared with proteins > 25 kDa MW, which were less easy to express (61% success).