Format

Send to

Choose Destination
J Mol Biol. 2006 Feb 10;356(1):1-8. Epub 2005 Nov 21.

Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI.

Author information

1
Division of Structural Biology, German Research Centre for Biotechnology (GBF) Mascheroder Weg 1, D-38124 Braunschweig, Germany. hartmut.niemann@gbf.de

Abstract

We present a fusion system suited to determine the crystal structure of small disulfide-rich proteins. McoEeTI, a hybrid inhibitor cystine knot microprotein, was produced as a soluble fusion to a catalytically inactive variant of the RNAse barnase in Escherichia coli. Functioning as a versatile tag, barnase facilitated purification, crystallization and high-resolution structure determination. Flexibility of the linker region allows for different relative orientations of barnase and the fusion partner in two crystallographically independent molecules and may thereby facilitate crystal packing. Nevertheless, the linker region is well ordered in both molecules. This system may prove more generally useful to determine the crystal structure of peptides and small proteins.

PMID:
16337652
DOI:
10.1016/j.jmb.2005.11.005
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center