Lipopolysaccharide stabilizes the crystal packing of the ABC transporter MsbA

Journal Article · Fri Jul 01 04:00:00 EDT 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309105016969· OSTI ID:22356149

Reyes, Christopher L.; Chang, Geoffrey ^[1]

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1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road CB105, La Jolla, CA 92137 (United States)

The use of lipopolysaccharide in the crystallization of the integral membrane protein MsbA was critical to the overall stability of the crystals and led to an increase in diffraction resolution. The ABC transporter MsbA is an integral membrane protein involved in the transport of lipid A and lipopolysaccharides to the outer leaflet of the inner membrane in bacteria. Here, the critical role of the natural substrate lipopolysaccharide in the crystallization and diffraction quality of MsbA crystals is reported. Initial crystals grown in complex with ATP–vanadate alone diffracted to ∼9 Å. Screening of the natural substrate lipopolysaccharides led to the crystallization of MsbA in complex with ADP–vanadate and Ra lipopolysaccharide. The increased order within the crystal lattice allowed structure determination to 4.2 Å.

• OSTI ID: 22356149
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL LATTICES
CRYSTALLIZATION
CRYSTALS
DIFFRACTION
LIPIDS
MEMBRANES
RESOLUTION
SCREENING
STABILITY
STOWING
SUBSTRATES