| Literature DB >> 27599857 |
Michael D Jones1, Anson C K Chan1, John F Nomellini1, Michael E P Murphy1, John Smit1.
Abstract
Protein surface layers are self-assembling, paracrystalline lattices on the surface of many prokaryotes. Surface-layer proteins have not benefited from widespread structural analysis owing to their resistance to crystallization. Here, the successful expression of a truncated version of RsaA, the surface-layer protein from Caulobacter crescentus, from a Caulobacter protein-expression system is reported. The purification, crystallization and initial X-ray diffraction analysis of the truncated RsaA, the largest surface-layer protein studied to date and the first from a Gram-negative bacterium, are also reported.Entities:
Keywords: Gram-negative; RTX motif; S-layer; phasing; surface-layer protein
Mesh:
Substances:
Year: 2016 PMID: 27599857 PMCID: PMC5012206 DOI: 10.1107/S2053230X16011638
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056