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Crystallization and X-ray analysis of monodisperse human properdin

DOI: 10.1107/S2053230X18018150 DOI Help

Authors: Dennis Vestergaard Pedersen (Aarhus University) , Margot Revel (Aarhus University) , Trine Amalie Fogh Gadeberg (Aarhus University) , Gregers Rom Andersen (Aarhus University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 75

State: Published (Approved)
Published: February 2019
Diamond Proposal Number(s): 13062

Abstract: The 54 kDa protein properdin, also known as factor P (FP), plays a major role in the complement system through the stabilization of the alternative pathway convertases. FP circulates in the blood as cyclic dimers, trimers and tetramers, and this heterogeneity challenges detailed structural insight into the mechanism of convertase stabilization by FP. Here, the generation of an intact FP monomer and a variant monomer with the third thrombospondin repeat liberated is described. Both FP monomers were excised from recombinant full-length FP containing internal cleavage sites for TEV protease. These FP monomers could be crystallized, and complete data sets extending to 2.8 Å resolution for the intact FP monomer and to 3.5 Å resolution for the truncated variant were collected. The principle of specific monomer excision and domain removal by the insertion of a protease cleavage site may be broadly applicable to structural studies of oligomeric, flexible and modular proteins.

Keywords: complement; properdin; modular proteins; crystallization

Subject Areas: Biology and Bio-materials

Beamlines: I02-Macromolecular Crystallography

Other Synchrotrons: European Synchrotron Radiation Facility; PETRA III