Crystallization and preliminary crystallographic studies of human septin 1 with site-directed mutations

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Hao HuRu-Chang Bi

Abstract

Septin 1 is a member of an evolutionarily conserved family of GTP-binding and filament-forming proteins named septins, which function in diverse processes including cytokinasis, vesicle trafficking, apoptosis, remodelling of the cytoskeleton, infection, neurodegeneration and neoplasia. Human septin 1 has been expressed and purified, but suffers from severe aggregation. Studies have shown that septin 1 with site-directed mutations of five serine residues (Ser19, Ser206, Ser307, Ser312 and Ser315) has a much lower degree of aggregation and better structural homogeneity and that the mutations cause only slight perturbations in the secondary structure of septin 1. This septin 1 mutant was crystallized and diffraction data were collected to 2.5 A resolution. The space group is P422, with unit-cell parameters a = b = 106.028, c = 137.852 A.

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Citations

Feb 5, 2008·Current Opinion in Cell Biology·Yves Barral, Makoto Kinoshita
Oct 16, 2019·Cytoskeleton·Michael A McMurray, Jeremy Thorner

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