Fusion-protein-assisted protein crystallization
Author(s)
Kobe, Bostjan
Ve, Thomas
Williams, Simon J
Griffith University Author(s)
Year published
2015
Metadata
Show full item recordAbstract
Fusion proteins can be used directly in protein crystallization to assist
crystallization in at least two different ways. In one approach, the ‘heterologous
fusion-protein approach’, the fusion partner can provide additional surface area
to promote crystal contact formation. In another approach, the ‘fusion of
interacting proteins approach’, protein assemblies can be stabilized by
covalently linking the interacting partners. The linker connecting the proteins
plays different roles in the two applications: in the first approach a rigid linker is
required to reduce conformational heterogeneity; in the second, conversely, ...
View more >Fusion proteins can be used directly in protein crystallization to assist crystallization in at least two different ways. In one approach, the ‘heterologous fusion-protein approach’, the fusion partner can provide additional surface area to promote crystal contact formation. In another approach, the ‘fusion of interacting proteins approach’, protein assemblies can be stabilized by covalently linking the interacting partners. The linker connecting the proteins plays different roles in the two applications: in the first approach a rigid linker is required to reduce conformational heterogeneity; in the second, conversely, a flexible linker is required that allows the native interaction between the fused proteins. The two approaches can also be combined. The recent applications of fusion-protein technology in protein crystallization from the work of our own and other laboratories are briefly reviewed.
View less >
View more >Fusion proteins can be used directly in protein crystallization to assist crystallization in at least two different ways. In one approach, the ‘heterologous fusion-protein approach’, the fusion partner can provide additional surface area to promote crystal contact formation. In another approach, the ‘fusion of interacting proteins approach’, protein assemblies can be stabilized by covalently linking the interacting partners. The linker connecting the proteins plays different roles in the two applications: in the first approach a rigid linker is required to reduce conformational heterogeneity; in the second, conversely, a flexible linker is required that allows the native interaction between the fused proteins. The two approaches can also be combined. The recent applications of fusion-protein technology in protein crystallization from the work of our own and other laboratories are briefly reviewed.
View less >
Journal Title
Acta Crystallographica Section F: Structural Biology Communications
Volume
F71
Subject
Biochemistry and cell biology not elsewhere classified