Abstract
Crystals of mutant carboxypeptidase T from Thermoactinomyces vulgaris (CPT11QG)with amino acid substitutions L211Q, T262S, L254S, and A251S were grown by the hanging-drop vapor-diffusion method. The crystals belong to sp. gr. P6(3)22. The X-ray-diffraction-data set,suitable for the crystal-structure determination at 2.6 Å resolution,was collected from the grown crystals at the ID23-1 beamline of the European Synchrotron Radiation Facility (ESRF, France).
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Funding
This study was financially supported by the Russian Foundation for Basic Research (project no. 19-04-00220; protein isolation and purification and the crystal growth in microgravity) and the Ministry of Science and Higher Education of the Russian Federation within the framework of the state assignment for the Federal Scientific Research Centre “Crystallography and Photonics” of the Russian Academy of Sciences (X-ray-diffraction-data collection and processing).
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Translated by T. Safonova
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Akparov, V.K., Konstantinova, G.E., Timofeev, V.I. et al. Preparation, Crystallization, and Preliminary X-Ray Diffraction Study of Mutant Carboxypeptidase T Bearing the Hydrophilized Primary Specificity Pocket. Crystallogr. Rep. 66, 476–478 (2021). https://doi.org/10.1134/S1063774521030020
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DOI: https://doi.org/10.1134/S1063774521030020