ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Expression, refolding, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgE.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- 7.10 MAG. A Novel Host Monoacylglyceride forCrystal growth & design · 2024Article
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Structural basis for alginate secretion across the bacterial outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl.Frontiers in microbiology · 2011Article
- Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Membrane topology of outer membrane protein AlgE, which is required for alginate production in Pseudomonas aeruginosa.Applied and environmental microbiology · 2010Article
- AlgK is a TPR-containing protein and the periplasmic component of a novel exopolysaccharide secretin.Structure (London, England : 1993) · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
AlgE is an outer membrane protein present in alginate-producing (mucoid) Pseudomonas aeruginosa. AlgE has been overexpressed in insoluble inclusion bodies, purified under denaturing conditions and refolded in a buffer containing decyl beta-D-maltopyranoside. Purified refolded AlgE was detergent-exchanged into n-octyl tetraoxyethylene and diffraction-quality crystals were grown using the hanging-drop vapor-diffusion method. The crystals grew as small hexagons with unit-cell parameters a = 98.8, b = 156.8, c = 90.4 A, alpha = beta = gamma = 90.0 degrees . The crystals exhibited the symmetry of space group C222 and diffracted to a minimum d-spacing of 3.0 A. On the basis of the Matthews coefficient (V(M) = 3.28 A(3) Da(-1)), one molecule is estimated to be present in the asymmetric unit.
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Registered trials
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