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

Gumpena, Rajesh; Lountos, George T.; Waugh, David S.

doi:10.1107/S2053230X18009901

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

Journal Article · Wed Aug 29 00:00:00 EDT 2018 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X18009901· OSTI ID:1506492

Gumpena, Rajesh; Lountos, George T.; Waugh, David S.

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:: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)

Sponsoring Organization:: NIH

OSTI ID:: 1506492

Journal Information:: Acta Crystallographica. Section F, Structural Biology Communications, Journal Name: Acta Crystallographica. Section F, Structural Biology Communications Journal Issue: 9 Vol. 74; ISSN ACSFEN; ISSN 2053-230X

Publisher:: International Union of Crystallography

Country of Publication:: United States

Language:: ENGLISH

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