MBP-binding DARPins facilitate the crystallization of an MBP fusion protein
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 coli maltose-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.
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1467532
- Journal Information:
- Acta Crystallographica. Section F, Structural Biology Communications, Journal Name: Acta Crystallographica. Section F, Structural Biology Communications Vol. 74 Journal Issue: 9; ISSN 2053-230X
- Publisher:
- International Union of Crystallography (IUCr)Copyright Statement
- Country of Publication:
- United Kingdom
- Language:
- English
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