Open AccessCrystallization and preliminary X‐ray diffraction of malate dehydrogenase from Plasmodium falciparum
Author(s) -
Wrenger Carsten,
Müller Ingrid B.,
Butzloff Sabine,
Jordanova Rositsa,
Lunev Sergey,
Groves Matthew R.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112014571
Subject(s) - malate dehydrogenase , plasmodium falciparum , crystallization , diffraction , x ray , monomer , x ray crystallography , enzyme , crystallography , chemistry , biology , biochemistry , physics , polymer , organic chemistry , quantum mechanics , malaria , optics , immunology
The expression, purification, crystallization and preliminary X‐ray diffraction characterization of malate dehydrogenase (MDH) from the malarial parasite Plasmodium falciparum ( Pf MDH) are reported. In order to gain a deeper understanding of the function and role of Pf MDH, the protein was purified to homogeneity. The purified protein crystallized in space group P 1, with unit‐cell parameters a = 72, b = 157, c = 159 Å, α = 105, β = 101, γ = 95°. The resulting crystals diffracted to a maximal resolution of 2.24 Å and the structure has been solved by molecular replacement, with 16 monomers in the asymmetric unit. The 16 monomers are arranged into four independent tetramers, in agreement with previous reports demonstrating the tetrameric solution state of Pf MDH. The X‐ray structure of Pf MDH is expected to clarify the differences in catalysis by Pf MDH compared with other MDH family members and to provide a basis for the structure‐based design of specific Pf MDH inhibitors as well as general MDH inhibitors.