Expression, crystallization and preliminary X-ray crystallographic analysis of glucose-6-phosphate dehydrogenase from the human pathogen Trypanosoma cruzi in complex with substrate. Corrigendum
aRedox Biology of Trypanosomes Laboratory, Institut Pasteur de Montevideo, Mataojo 2020, 11400 Montevideo, Uruguay, bUnit of Protein Crystallography, Institut Pasteur de Montevideo, Mataojo 2020, 11400 Montevideo, Uruguay, cBiochemistry Department, Universidad de la República, Avenida General Flores 2125, 11800 Montevideo, Uruguay, and dDepartment of Structural Biology and Chemistry, Institut Pasteur, 25 Rue du Dr Roux, 75015 Paris, France
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A figure in the article by Ortíz et al. [(2011), Acta Cryst. F67, 1457–1461] is corrected.
In Fig. 1 of the article by Ortíz et al. (2011), the amino-acid sequence shown for T. cruzi G6PDH corresponds to isoform 2 (accession No. Q1WBU5) and not to the protein used in the study, namely isoform 1 (accession No. Q4E0B2). The correct sequence is shown here in Fig. 1 and the four residues that are different between the two protein sequences are highlighted with a black dot: E/Q, Y/H, H/Y and I/S for isoform 1/isoform 2. The N-terminal extension, absent in the truncated mutant Δ37N, is shown as an insertion fragment in the top of the panel. The N-terminal stretch incorporated as a fusion from the expression vector, is indicated in bold red. Identical residues with respect to the human enzyme (accession No. P11413) are shown on a black background, while conservative substitutions are highlighted with a grey background. The cofactor and substrate-binding sites are depicted with asterisks and crosses, respectively.
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