Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX

Journal Article · Sat May 01 00:00:00 EDT 2010 · Acta Crystallographica F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309110011851· OSTI ID:1014302

Weadge, J T; Robinson, H; Yip, P P; Arnett, K; Tipton, P A; Howell, P L

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 = 86.9 {angstrom}, {beta} = 95.7{sup o}. The crystals exhibited the symmetry of space group P2{sub 1} and diffracted to a minimum d-spacing of 2.1 {angstrom}. On the basis of the Matthews coefficient (V{sub M} = 2.25 {angstrom}{sup 3} Da{sup -1}), two molecules were estimated to be present in the asymmetric unit.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States)
• Sponsoring Organization: DOE - OFFICE OF SCIENCE
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 1014302
• Report Number(s): BNL-93660-2010-JA; R&D Project: BO-070; KP1605010; TRN: US201111%%255
• Journal Information: Acta Crystallographica F: Structural Biology and Crystallization Communications, Vol. 66, Issue 5; ISSN 1744-3091
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
ALGINATES
AZOTOBACTER
CRYSTALLIZATION
PLATES
PRODUCTION
PROTEINS
PSEUDOMONAS
PURIFICATION
SPACE GROUPS
SYMMETRY