ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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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2 citing papers in PubMed, 5 citations in OpenAlex.
- Microseed matrix screening for optimization in protein crystallization: what have we learned?Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystallization screening: the influence of history on current practice.Acta crystallographica. Section F, Structural biology communications · 2014Review
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5 authors at 2 institutions in 2 countries.
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Abstract
Arginase (EC 3.5.3.1) is an aminohydrolase that acts on L-arginine to produce urea and ornithine. Two isotypes of the enzyme are found in humans. Type I is predominantly produced in the liver and is a homotrimer of 35 kDa subunits. Human arginase (hArginase) I is seen to be up-regulated in many diseases and is a potential therapeutic target for many diverse indications. Previous reports of crystallization and structure determination of hArginase have always included inhibitors of the enzyme: here, the first case of a true apo crystal form of the enzyme which is suitable for small-molecule soaking is reported. The crystals belonged to space group P2(1)2(1)2(1) and have approximate unit-cell parameters a=53, b=67.5, c=250 Å. The crystals showed slightly anisotropic diffraction to beyond 2.0 Å resolution.
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