Open AccessProduction, purification, crystallization and preliminary X‐ray diffraction studies of the nucleoside diphosphate kinase b from Leishmania major
Author(s) -
Tonoli Celisa Caldana Costa,
Vieira Plinio Salmazo,
Ward Richard John,
Arni Raghuvir Krishnaswamy,
De Oliveira Arthur Henrique Cavalcante,
Murakami Mario Tyago
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109037567
Subject(s) - nucleoside diphosphate kinase , kinase , nucleotide salvage , escherichia coli , crystallization , biology , nucleoside , biochemistry , leishmania , parasite hosting , crystallography , nucleotide , chemistry , biophysics , gene , organic chemistry , world wide web , computer science
Nucleoside diphosphate kinases (NDKs; EC 2.7.4.6) play an essential role in the synthesis of nucleotides from intermediates in the salvage pathway in all parasitic trypanosomatids and their structural studies will be instrumental in shedding light on the biochemical machinery involved in the parasite life cycle and host–parasite interactions. In this work, NDKb from Leishmania major was overexpressed in Escherichia coli , purified to homogeneity and crystallized using the sitting‐drop vapour‐diffusion method. The NDK crystal diffracted to 2.2 Å resolution and belonged to the trigonal crystal system, with unit‐cell parameters a = 114.2, c = 93.9 Å. Translation‐function calculations yielded an unambiguous solution in the enantiomorphic space group P 3 2 21.