ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Crystallization and preliminary X-ray diffraction studies of maleylacetate reductase from Rhizobium sp. strain MTP-10005.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed, 3 citations in OpenAlex.
- Expression, purification, crystallization and preliminary X-ray analysis of maleylacetate reductase from Burkholderia sp. strain SJ98.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
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Authors and funding
5 authors at 3 institutions in 1 country.
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Abstract
Maleylacetate reductase (EC 1.3.1.32), which catalyzes the reduction of maleylacetate to 3-oxoadipate, plays an important role in the aerobic microbial catabolism of resorcinol. The enzyme has been crystallized at 293 K by the sitting-drop vapour-diffusion method supplemented with a microseeding technique, using ammonium sulfate as the precipitating agent. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 56.85, b = 121.13, c = 94.09 A, beta = 101.48 degrees , and contained one dimeric molecule in the asymmetric unit. It diffracted to 1.79 A resolution.
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