ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Crystallization and preliminary X-ray crystallographic analysis of a helicase-like domain from a tomato mosaic virus replication protein.
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, 3 citations in OpenAlex.
- Binding studies between cytosinpeptidemycin and the superfamily 1 helicase protein of tobacco mosaic virus.RSC advances · 2018Article
- Crystal structure of the superfamily 1 helicase from Tomato mosaic virus.Journal of virology · 2012Article
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11 authors at 4 institutions in 1 country.
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Abstract
Tomato mosaic virus belongs to the genus Tobamovirus in the alphavirus-like superfamily of positive-strand RNA viruses. The alphavirus-like superfamily includes many plant and animal viruses of agronomical and clinical importance. These viruses encode replication-associated proteins that contain a putative superfamily 1 helicase domain. No three-dimensional structures for this domain have been determined to date. Here, the crystallization and preliminary X-ray diffraction analysis of the 130K helicase domain are reported. Diffraction data were collected and processed to 2.05 and 1.75 Å resolution from native and selenomethionine-labelled crystals, respectively. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 85.8, b = 128.3, c = 40.7 Å.
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