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 (EcLptC24-191G153R).

Protein Crystallization of Two Recombinant Lpt Proteins / M. Bollati, L.J. Gourlay (METHODS IN MOLECULAR BIOLOGY). - In: Lipopolysaccharide Transport / [a cura di] P. Sperandeo. - Prima edizione. - [s.l] : Springer, 2022. - ISBN 978-1-0716-2580-4. - pp. 249-263 [10.1007/978-1-0716-2581-1_15]

Protein Crystallization of Two Recombinant Lpt Proteins

M. Bollati
Primo
;
L.J. Gourlay
Ultimo
2022

Abstract

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 (EcLptC24-191G153R).
E. coli; Lipopolysaccharide transport protein; Outer membrane biogenesis; Protein crystallization; Vapor diffusion; Carrier Proteins; Crystallization; Crystallography, X-Ray; Escherichia coli; Membrane Proteins; Recombinant Proteins; Escherichia coli Proteins; Lipopolysaccharides;
Settore BIO/10 - Biochimica
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/940747
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