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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(69), p. 669-672, 2013

DOI: 10.1107/s1744309113012165

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Heterogeneous nucleation helps the search for initial crystallization conditions of γ-glutamyl transpeptidase fromBacillus licheniformis

Journal article published in 2013 by Long-Liu Lin, Antonello Merlino ORCID
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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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 P212121, 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.