Crystallization and preliminary X‐ray diffraction studies of Tyr167His mutant α‐cyclodextrin glucanotransferase from Bacillus macerans. Issue 10 (8th October 2013)

• Record Type: Journal Article
• Authors: Yue, Yang; Liu, Shengquan; Li, Hongbin; Song, Binghong; Xie, Ting; Sun, Yan; Chao, Yapeng; Qian, Shijun
• Is Part Of: Acta crystallographica. Volume 69:Issue 10(2013:Oct.)
• Page Start: 1186
• Page End: 1189
• Publication Date: 2013-10-08
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113024810
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Improving the specificity of α‐cyclodextrin glucanotransferase is a significant issue in the field of α‐cyclodextrin production. In this study, a constructed Y167H mutant α‐cyclodextrin glucanotransferase with enhanced α‐cyclodextrin specificity was successfully expressed and purified. Single crystals were grown using PEG 4000 as a precipitating agent by the hanging‐drop vapour‐diffusion method at 293 K. The crystals exhibited two kinds of morphology in different crystallization conditions. The crystals diffracted to at least 2.2 Å resolution (space group <italic>P</italic>2₁2₁2₁), with unit‐cell parameters <italic>a</italic> = 65.69, <italic>b</italic> = 78.70, <italic>c</italic> = 137.00 Å. Assuming the asymmetric cell to be occupied by a monomer of 75 kDa, the unit cell contains 43.77% solvent with a crystal volume per protein mass, <italic>V</italic>_M, of 2.19 ų Da⁻¹.</p> </abstract>