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The crystal structure of a monomeric mutant of Azami-Green (mAG) from G. fascicularis was determined at 2.2 Å resolution.
The first crystal structure of phosphoglucose isomerase from M. tuberculosis H37Rv is reported.
The crystal structure of OPRTase from the caries pathogen Streptococcus mutans is reported at 2.4 Å resolution.
In order to determine the structure–function relationship of the azo-dye reduction mechanism, an X-ray crystallographic study of azoreductases was performed. Selenomethionine-labelled AzrA (SeMet-AzrA) and AzrC were crystallized by the hanging-drop vapour-diffusion method.
The purification, crystallization and preliminary X-ray crystallographic analysis of glyceraldehyde-3-phosphate dehydrogenase 1 (GAP1) from MRSA252 in the apo form is reported.
A female-specific lacrimal protein from Syrian hamsters has been crystallized by the sitting-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffraction data were collected to 1.86 Å resolution.
Crystals of C-terminally His-tagged ThyX from H. pylori belonged to space group C2, with unit-cell parameters a = 221.92, b = 49.43, c = 143.02 Å, β = 98.84°, and diffracted to beyond 2.5 Å resolution.
N-terminal fragments of the cyclic AMP receptor protein from E. coli created by two different proteases, subtilisin and chymotrypsin, have been crystallized and diffracted to 2.0 and 2.8 Å resolution, respectively.
The endonuclease/exonuclease/phosphatase-homology domain of phosphodiesterase PDE12 has been crystallized. The crystals diffracted to 2.5 Å resolution.
Selenomethionine-derivatized glutamate dehydrogenase from P. asaccharolyticus has been crystallized. Diffraction data were collected to 3.5 Å resolution from crystals belonging to the rhombohedral space group H32 and structure determination is in progress.
H. pylori MinE has been expressed, purified and crystallized. Native and MAD data sets have been collected from H. pylori MinE crystals to 2.8 and 3.0 Å resolution, respectively.
The SMU.2055 gene from the major caries pathogen Streptococcus mutans was cloned and native and SeMet-labelled SMU.2055 proteins were expressed at a high level. Diffraction-quality crystals of SeMet-labelled SMU.2055 were obtained using the sitting-drop vapour-diffusion method and diffracted to a resolution of 2.5 Å.
Two soluble His-tagged forms of the lytic transglycosylase MltF, one containing full length protein, the other containing its N-terminal domain, have been successfully overexpressed, purified and crystallized. X-ray diffraction data were collected for both crystal forms, including a MAD data set to 2.7 Å for the MltF N-terminal domain.
Triclinic crystals of a self-complementary DNA heptacosamer with 20-base-pair duplexes flanked by 3′-terminal seven-nucleotide overhangs have been obtained. X-ray data were collected to 2.8 Å resolution using synchrotron radiation.
The N-terminal carbohydrate-recognition domain of human galectin-4 has been crystallized by the vapour-diffusion technique using polyethylene glycol as the precipitant agent. A complete data set was collected from a native crystal to 2.2 Å resolution.
A soluble domain spanning amino-acid residues 16–197 of the Drosophila Dribble protein was overexpressed in E. coli, purified and crystallized. X-ray diffraction data were collected to beyond 2 Å resolution.
The Fe2+-dependent dioxygenase NicX from P. putida KT2440 has been crystallized using the vapour-diffusion method. Native data have been collected to 2.0 Å resolution.
The macrophage growth locus A (MglA) protein from F. tularensis crystallized in the hexagonal space group P61 or P65, with unit-cell parameters a = b = 125, c = 54 Å.
Crystals of infectious West Nile virus were obtained and diffracted at best to about 25 Å resolution. Preliminary analysis of the diffraction pattern suggested tight hexagonal packing of the intact virus.
The RNA-binding protein Hfq from B. subtilis was crystallized using the hanging-drop vapour-diffusion method in two crystal forms that belonged to space groups I422 and F222; diffraction data were collected to 2.2 Å resolution from both forms.
The N-terminal domain of ING4 was overexpressed in Escherichia coli and purified to homogeneity. Crystallization experiments yielded crystals that were suitable for high-resolution X-ray diffraction analysis.
Glyoxalase I from L. infantum was cloned, overexpressed in E. coli, purified and crystallized.
The expression, purification and crystallization of S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, an essential enzyme from the folate-biosynthesis pathway, is reported.
The expression, purification and crystallization of nosiheptide-resistance methyltransferase (NSR) from Streptomyces actuosus is described.
The expression, purification and crystallization of Plasmodium actin-depolymerization factors 1 and 2 are described. X-ray diffraction data were collected to 2.0 and 2.1 Å resolution, respectively, and the structures of both proteins in solution were characterized.
The expression, purification and crystallization of the periplasmic protein AlgX from P. aeruginosa is described. The crystals diffracted to 2.1 Å resolution.
Champedak mannose-binding lectin was crystallized at 293 K. Crystallization conditions and preliminary X-ray diffraction analysis are reported.
Rabbit muscle aldolase (RMA) was crystallized in complex with the low-complexity domain (LC4) of sorting nexin 9. Monoclinic crystals were obtained at room temperature that displayed large mosaicity and poor X-ray diffraction. However, orthorhombic RMA–LC4 crystals grown at 277 K under similar conditions exhibited low mosaicity, allowing data collection to 2.2 Å Bragg...
The cloning, purification, crystallization and preliminary crystallographic studies of three DsbA-like proteins present in S. enterica serovar Typhimurium, SeDsbA, SeDsbL and SeSrgA, are reported.
Diffraction-quality crystals of I. hospitalis neelaredoxin have been produced. The cloning, expression, purification, crystallization and X-ray crystallographic analysis are reported.
To determine the binding mechanism of BoNT/OFD05 and its ganglioside receptors on neuronal cells, recombinant BoNT/OFD05 receptor-binding domain has been expressed, purified and crystallized.
Crystallization and preliminary X-ray crystallographic analysis of the tetracycline-degrading monooxygenase TetX2 from B. thetaiotaomicron are reported.
A simple ‘melt test’ to distinguish salt crystals from macromolecule crystals is described.