Protein Crystallization of Two Recombinant Lpt Proteins.

Autor: Bollati M; Department of Biosciences, Università degli Studi di Milano, Milan, Italy.; Institute of Biophysics - CNR, Milan, Italy., Gourlay LJ; Department of Biosciences, Università degli Studi di Milano, Milan, Italy. louise.gourlay@unimi.it.
Jazyk: angličtina
Zdroj: Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2022; Vol. 2548, pp. 249-263.
DOI: 10.1007/978-1-0716-2581-1_15
Abstrakt: The prerequisite for 3D structure determination of macromolecules via X-ray crystallography is well-ordered, diffracting crystals. Here, we report the recombinant production, biophysical/biochemical protein sample characterization, and vapor diffusion sitting drop crystallization protocols for two lipopolysaccharide transport proteins: LptH from Pseudomonas aeruginosa (Pa-LptH) and an inactive LptC mutant (G153R) from Escherichia coli (EcLptC 24-191 G153R).
(© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE