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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Crystallization and Crystallographic Analyses of Triosephosphate Isomerase from Naegleria gruberi

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Penteado, R. F. [1] ; Martini, V. P. [2] ; Iulek, J. [1]
Total Authors: 3
[1] Univ Estadual Ponta Grossa, Dept Quim, Lab Purificacao Prot, Campus Uvaranas, Av Gen Carlos Cavalcanti 4748, BR-84030900 Ponta Grossa, PR - Brazil
[2] Inst Fed Parana, Rua Pedro Koppe 100, BR-84500000 Irati, PR - Brazil
Total Affiliations: 2
Document type: Journal article
Source: REVISTA VIRTUAL DE QUIMICA; v. 8, n. 6, p. 1835-1841, 2016.
Web of Science Citations: 0

The enzyme Triosephosphate Isomerase (TIM) from Naegleria gruberi is involved in the glycolytic pathway, in which it acts upon the conversion of dihydroxyacetone phosphate to D-glyceraldehyde 3-phosphate. Currently, the most similar TIM with 3D structure reported is from the plant Arabidopsis thaliana, which has 58% sequence identity with NgTIM. Recombinant NgTIM protein was expressed in E. coli BL21(DE3), purified by affinity and size exclusion chromatographies and crystallized by the vapor diffusion method. The best crystals were obtained in 3 different conditions, the one to provide the best dataset in ethanol 15% (V/V) and pentaerythritol propoxylate 40% (V/V). X ray diffraction data were collected for this crystal at 2.64 angstrom resolution and processed. It belongs to the space group P4(1)22 and have unit cell parameters a = 79.70, c = 98.11 angstrom. The asymmetric unit contains one monomer, with V-M of 2.68 angstrom 3 Da(-1) and a solvent content of 54.2 %. (AU)

FAPESP's process: 08/57910-0 - National Institute of Structural Biotechnology and Medicinal Chemistry in Infectious Diseases
Grantee:Richard Charles Garratt
Support type: Research Projects - Thematic Grants