The crystal structure of the Z-isomer of 2,4-diamino-5-[2-(2′-methoxyphenyl)-propenyl]-furo[2,3-d]pyrimidine shows an unusual packing arrangement in which the conserved active site Arg70 forms a salt bridge to the side chain of Glu44 from a symmetry-related molecule.
Haemoglobin from Camelus dromedarius provides an interesting case study of adaptation to life in deserts at extremely high temperatures. An ambition to unravel the integrated structural and functional aspects of the casual survival of this animal at high temperatures led the authors to specifically work on this problem. This work reports the preliminary crystallographic study of camel haemoglobin.
In this study, the PaaX-like protein from the hyperthermophilic archaeon Sulfolobus solfataricus P2 was successfully crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant.
Crystallization of the ligand–receptor complex of GDF5 and its type I receptor BRIB requires the presence of the activin type IIB receptor (ActRIIB) for crystal formation, but ActRIIB is not part of the complex found in the asymmetric unit.
The truncated cytosolic domain of the iron transporter FeoB from T. maritima was overexpressed, purified and crystallized. Four native or SeMet crystal forms in a nucleotide-free state or in complex with either GDP or GMPPNP diffracted to resolutions of between 1.5 and 2.1 Å.
Expression, purification, crystallization, and preliminary X-ray diffraction analysis of the DNA-binding effector domain from an atypical OmpR response regulator homolog, ChxR, encoded by Chlamydia trachomatis are reported.
In order to better elucidate the functions of FlgD in flagellar hook biosynthesis, the three-dimensional structure of FlgD is being determined by X-ray crystallography. Here, the expression, purification, crystallization and preliminary crystallographic analysis of FlgD from P. aeruginosa are reported.
A completely `all-locked' nucleic acid duplex was designed from an E. coli tRNASer microhelix. The helix consists exclusively of LNA building blocks and was crystallized. The crystals diffracted to 1.9 Å resolution.
The DEAD-box protein Mss116p was crystallized in a complex with a U10 RNA oligonucleotide and an ATP analog. High glycerol (50%) and L-arginine plus L-glutamate (50 mM each) enabled the concentration of Mss116p to ∼10 mg ml−1 for crystallization.
The sulfide:quinone oxidoreductase from A. ferrooxidans ATCC 23270 was overexpressed in E. coli and purified. Crystallization and preliminarily X-ray crystallographic analysis were performed for the recombinant enzyme.
Crystals of a complex formed between the 59 kDa N-terminal fragment of the E. coli DNA gyrase A subunit and the antibiotic simocyclinone D8 were obtained and X-ray data were recorded to a resolution of 2.75 Å.
The Mms21–Smc5 protein complex has been crystallized. The diffraction of the crystals was improved greatly by glutaraldehyde treatment and X-ray diffraction data sets were collected to resolutions of 2.3 and 3.9 Å from native and selenomethionine-derivative protein crystals, respectively.