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MBP-binding DARPins facilitate the crystallization of an MBP fusion protein

Journal Article · · Acta Crystallographica. Section F, Structural Biology Communications

The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner,Escherichia colimaltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
National Institutes of Health (NIH)
OSTI ID:
1506492
Journal Information:
Acta Crystallographica. Section F, Structural Biology Communications, Vol. 74, Issue 9; ISSN 2053-230X
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
ENGLISH

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