ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006
The purification, crystallization and preliminary diffraction of a glycerophosphodiesterase from Enterobacter aerogenes.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- X-ray Scattering Studies of Protein Structural Dynamics.Chemical reviews · 2017Review
- Predicting X-ray diffuse scattering from translation-libration-screw structural ensembles.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
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5 authors.
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Abstract
The metallo-glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) has been cloned, expressed in Escherichia coli and purified. Initial screening of crystallization conditions for this enzyme resulted in the identification of needles from one condition in a sodium malonate grid screen. Removal of the metals from the enzyme and subsequent optimization of these conditions led to crystals that diffracted to 2.9 angstroms and belonged to space group P2(1)3, with unit-cell parameter a = 164.1 angstroms. Self-rotation function analysis and V(M) calculations indicated that the asymmetric unit contains two copies of the monomeric enzyme, corresponding to a solvent content of 79%. It is intended to determine the structure of this protein utilizing SAD phasing from transition metals or molecular replacement.
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