Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of an archaeal protein homologous to plant nicotianamine synthase
Author(s) -
Dreyfus Cyril,
Pignol David,
Arnoux Pascal
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108027796
Subject(s) - dimer , crystallization , monomer , chemistry , polyethylene glycol , biochemistry , atp synthase , chelation , crystallography , enzyme , organic chemistry , polymer
In plants, nicotianamine synthase (NAS) plays a key role in metal homeostasis as it catalyzes the formation of nicotianamine, an important iron and nickel chelator and a precursor of plant phytosiderophores. Here, the crystallization of a protein from Methanothermobacter thermoautotrophicus (MTH675; referred to here as MtNAS) that appears to be homologous to plant NAS is reported. Purification of this protein showed a monomer–dimer equilibrium that could be displaced by using a reducing agent such as DTT. Crystals belonging to space group P 2 1 2 1 2 1 and containing dimers of MtNAS were grown by the vapour‐diffusion method using polyethylene glycol 3350 as precipitant. A complete native X‐ray data set was collected to 1.7 Å resolution at a synchrotron source.