ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and preliminary X-ray diffraction studies of infectious bronchitis virus nonstructural protein 9.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. 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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1 citing paper in PubMed, 1 citations in OpenAlex.
- Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9.Protein science : a publication of the Protein Society · 2017Article
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6 authors at 3 institutions in 1 country.
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Abstract
Avian infectious bronchitis virus (IBV), which causes respiratory disease in infected birds, belongs to coronavirus group 3. IBV encodes 15 nonstructural proteins (nsp2-nsp16) which play crucial roles in RNA transcription and genome replication. Nonstructural protein 9 (nsp9) has been identified as a protein that is essential to viral replication because of its single-stranded RNA-binding ability. The gene segment encoding IBV nsp9 has been cloned and expressed in Escherichia coli. The protein has been crystallized and the crystals diffracted X-rays to 2.44 A resolution. They belonged to the cubic space group I432, with unit-cell parameters a = b = c = 123.4 A, alpha = beta = gamma = 90 degrees . The asymmetric unit appeared to contain one molecule, with a solvent content of 62% (V(M) = 3.26 A(3) Da(-1)).
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