Ariza, A. orcid.org/0000-0003-4364-823X, Vickers, T.J., Greig, N. et al. (2 more authors) (2005) Crystallization and preliminary X-ray analysis of Leishmania major glyoxalase I. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 61 (8). pp. 769-772. ISSN 1744-3091
Abstract
Glyoxalase I (GLO1) is a putative drug target for trypanosomatids, which are pathogenic protozoa that include the causative agents of leishmaniasis. Significant sequence and functional differences between Leishmania major and human GLO1 suggest that it may make a suitable template for rational inhibitor design. L. major GLO1 was crystallized in two forms: the first is extremely disordered and does not diffract, while the second, an orthorhombic form, produces diffraction to 2.0 Å. Molecular-replacement calculations indicate that there are three GLO1 dimers in the asymmetric unit, which take up a helical arrangement with their molecular dyads arranged approximately perpendicular to the c axis. Further analysis of these data are under way.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2005 International Union of Crystallography. This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (https://creativecommons.org/licenses/by/2.0/legalcode) which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are properly cited. |
Keywords: | Animals; Crystallization; Lactoylglutathione Lyase; Leishmania major; Models, Molecular; X-Ray Diffraction |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 05 Jul 2023 16:30 |
Last Modified: | 05 Jul 2023 16:30 |
Status: | Published |
Publisher: | International Union of Crystallography (IUCr) |
Refereed: | Yes |
Identification Number: | 10.1107/s174430910502169x |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:201232 |