Expression, Purification, Crystallization and Preliminary X-Ray Analysis of Pseudomonas aeuginosa AlgX

Authors

Joel T. Weadge, Wilfrid Laurier UniversityFollow
Patrick P. Yip, The Hospital for Sick Children
Howard Robinson, Brookhaven National Laboratory
Krista Arnett, University of Missouri-Columbia
Peter A. Tipton, University of Missouri-Columbia
P. Lynne Howell, University of Toronto

Document Type

Article

Publication Date

2010

Department

Biology

Abstract

AlgX is a periplasmic protein required for the production of the exopolysaccharide alginate in Pseudomonas sp. and Azotobacter vinelandii. AlgX has been overexpressed and purified and diffraction-quality crystals have been grown using iterative seeding and the hanging-drop vapor-diffusion method. The crystals grew as flat plates with unit-cell parameters a=46.4, b=120.6, c=86.9Å, β=95.7°. The cyrstals exhibited the symmetry of space group P2₁ and diffracted to a minimimum _d-spacing of 2.1Å. On the basis of the Matthews coefficient (V_M=2.25ų Da^-1), two molecules were estimated to be present in the asymmetric unit.

Comments

This article was originally published in Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(5): 588-591. © 2010 International Union of Crystallography

Recommended Citation

Weadge, Joel T.; Yip, Patrick P.; Robinson, Howard; Arnett, Krista; Tipton, Peter A.; and Howell, P. Lynne, "Expression, Purification, Crystallization and Preliminary X-Ray Analysis of Pseudomonas aeuginosa AlgX" (2010). Biology Faculty Publications. 43.
https://scholars.wlu.ca/biol_faculty/43