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 : Methods and Protocols / [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. BollatiPrimo
;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).
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