ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase from Bacillus licheniformis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. 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, 3 citations in OpenAlex.
- High Resolution X-ray Diffraction Dataset for Bacillus licheniformis Gamma Glutamyl Transpeptidase-acivicin complex: SUMO-Tag Renders High Expression and Solubility.The protein journal · 2017Article
- Heterogeneous nucleation is required for crystallization of the ZnuA domain of pneumococcal AdcA.Acta crystallographica. Section F, Structural biology communications · 2015Article
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2 authors at 2 institutions in 2 countries.
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Abstract
Here, the crystallization and preliminary X-ray diffraction studies of Bacillus licheniformis γ-glutamyl transpeptidase (BlGT) are reported. The serendipitous finding of heterogeneous nucleants in the initial experiments provided the first crystallization conditions for the protein. Crystals were grown by hanging-drop vapour diffusion using a precipitant solution consisting of 20%(w/v) PEG 3350, 0.2 M magnesium chloride hexahydrate, 0.1 M Tris-HCl pH 8.2. The protein crystallized in the orthorhombic space group P2(1)2(1)2(1), with one heterodimer per asymmetric unit and unit-cell parameters a = 60.90, b = 61.97, c = 148.24 Å. The BlGT crystals diffracted to 2.95 Å resolution.
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