Abstract
Crystals of recombinant human tumour necrosis factor, an 157 amino acid protein expressed in Escherichia coli, have been obtained that are suitable for a full structure determination. A dramatic increase in crystal size was obtained with the addition of the non-ionic detergent β-octyl glucoside. The crystals belong to the trigonal space group P3121 with unit cell dimensions a=b=166.0 å and c=93.0 å, and diffract to 2.9 å. Crystal density measurements indicated a solvent content of close to 65%. Since TNF has been proposed to exist at the trimer in solution, this is consistent with an arrangement of two independent trimers, i.e. six molecules, in the asymmetric unit.
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