ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Purification, crystallization and preliminary X-ray analysis of a hexameric beta-glucosidase from wheat.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. 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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2 citing papers in PubMed, 4 citations in OpenAlex.
- Dispersed benzoxazinone gene cluster: molecular characterization and chromosomal localization of glucosyltransferase and glucosidase genes in wheat and rye.Plant physiology · 2011Article
- Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye.Plant physiology · 2006Article
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8 authors at 2 institutions in 1 country.
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Abstract
The wheat beta-glucosidase TaGlu1b, which is only active in a hexameric form, was tagged with 6xHis at the N-terminus, overexpressed in Escherichia coli and purified in two steps. The protein complexed with a substrate aglycone was crystallized at 293 K from a solution containing 10 mM HEPES pH 7.2, 1 M LiSO4 and 150 mM NaCl using the hanging-drop vapour-diffusion method. Diffraction data were collected to 1.7 A at the Photon Factory. The crystal belongs to space group P4(1)32, with unit-cell parameters a = b = c = 194.65 A, alpha = beta = gamma = 90 degrees. The asymmetric unit was confirmed by molecular-replacement solution to contain one monomer, giving a solvent content of 72.1%.
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