|Home | About | Journals | Submit | Contact Us | Français|
An analysis of the protein–ligand interactions in two crystal structures of DHFR-TS from C. hominis reveals a possible structural basis for observed antifolate resistance in C. hominis DHFR. A comparison with the structure of human DHFR reveals residue substitutions that may be exploited for the design of species-selective inhibitors.
The crystal structure of the 26 kDa glutathione S-transferase from S. japonicum (SjGST) was determined at 3 Å resolution in the new space group P212121. The structure of orthorhombic SjGST reveals unique features of the ligand-binding site and dimer interface when compared with previously reported structures.
Crystallization and X-ray diffraction methods for native A. tumefaciens ADP-glucose pyrophosphorylase and its selenomethionyl derivative are described. Two crystal forms are identified, both of which diffract to 2 Å.
The crystallization of a hypothetical acetyltransferase from the archaeon P. furiosus by hanging-drop vapour diffusion is reported in space group P622.
The dhlIVa gene coding for DehIVa was expressed in Escherichia coli and the protein was purified and crystallized using the hanging-drop method.
A truncated soluble human semicarbazide-sensitive amine oxidase has been crystallized. Data were collected to 2.5 Å from a crystal suffering from twinning, pseudo-symmetry and anisotropy. The structure was solved in space group P43.
Crystals of the aspartate carbamoyltransferase of the psychrophile M. profunda diffract X-rays to 2.85 Å. Three catalytic and three regulatory subunits are predicted per asymmetric unit.
Human spliceosomal protein TXNL4B was purified and crystallized.
A high-affinity mutant CD8 (haCD8) has been developed with the aim of developing a therapeutic immunosuppressor. In order to fully understand the nature of the haCD8 interaction, this protein was crystallized using the sitting-drop vapour-diffusion method.
The crystallization and preliminary characterization of the family PL-7 alginate lyases A1-II and A1-II′ from Sphingomonas sp. A1 are presented.
Reducing-end-xylose releasing exo-oligoxylanase (Rex) from B. halodurans C-125 was crystallized. A diffraction data set was collected to 1.35 Å resolution.
A thermostable ribonuclease HIII from B. stearothermophilus (Bst RNase HIII) was crystallized and preliminary crystallographic studies were performed. Plate-like overlapping polycrystals were grown by the sitting-drop vapour-diffusion method at 283 K.
The mRNA-binding domain of M. thermoacetica selenocysteine-specific elongation factor SelB (residues 512–634, SelB-M) was overproduced in E. coli and its cognate mRNA ligand, 23 nucleotides of the SECIS RNA hairpin, was chemically prepared. The purified SelB-M–SECIS RNA complex has been crystallized in space group P21212 and diffracted to 2.3 Å.
Acetylene hydratase, a tungsten-containing hydroxylase that converts acetylene to acetaldehyde, has been purified and crystallized under anaerobic conditions.
A maltooligosaccharide-metabolizing enzyme from T. vulgaris R-47 (TGA) homologous to glucoamylase degrades maltooligosaccharides more efficiently than starch, unlike fungal glucoamylases. TGA was crystallized and the state of the protein in solution was analyzed by gel-filtration chromatography.
An open reading frame from E. coli MG1655 has been cloned, expressed and purified. Crystals obtained from the purified recombinant protein have been obtained in a variety of different forms diffracting to 1.8 Å resolution.
The psychrophilic protease Apa1 consisting of a subtilisin-like region and a large insert (148 residues) with unknown structure has been crystallized. Collection of a data set to 1.78 Å resolution and molecular-replacement searches are reported.
This paper describes the first crystallization study of a flavoprotein monooxygenase that can cleave an aromatic compound without requiring a metal-ion cofactor.
Two outer membrane factor family proteins, OprM and OprN, from a tripartite efflux pump found in P. aeruginosa were crystallized. A diffraction data set was collected to 3.8 Å resolution in the space group C2 for OprM crystals.
A human kynurenine aminotransferase II homologue from P. horikoshii OT3 has been overproduced in E. coli, purified, and characterized. Crystals of this protein have been obtained and analyzed by X-ray diffraction.
The hyperthermostable thioredoxin peroxidase from the aerobic hyperthermophilic archaeon A. pernix K1 was crystallized. The crystal diffracted to 2.7 Å resolution.
The first crystal structure of a Mimosoideae lectin, Parkia platycephala has been solved by MAD phasing using 5-bromo-4-chloro-3-indolyl-α-d-mannose as an anomalous X-ray scatterer. This strategy may be useful for structure elucidation of novel lectins or when molecular replacement methods fail.
The site-specific DNA nickase Nb.BspD6I has been crystallized in space group P21, with unit-cell parameters a = 57.76, b = 90.67, c = 71.71, β = 110.1°.
A protein disulfide oxidoreductase from A. pernix K1 has been crystallized for the first time. The crystals belong to space group I222 or I212121 and diffract to 1.93 Å resolution.