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Tyr131 plays an important role in determining the substrate specificity and thermal stability of azoreductase 1 from P. aeruginosa (pAzoR1). The structure shows that the substrate methyl red binds deeper in the active site of the mutant, which is reflected in the change in enzymic properties.
The crystal structure of the hypothetical protein YqgQ from B. subtilis is reported at 2.1 Å resolution.
Overexpression, purification, crystallization and preliminary X-ray diffraction of the stromal-cell-derived factor 2-like protein of Arabidopsis thaliana are reported. The crystals belonged to the space group P61 and diffracted to 1.95 Å resolution.
The MIF4G domain of DAP5 was crystallized in two distinct crystal forms. Diffraction patterns have been analyzed and preliminary analysis, including molecular replacement, is presented here.
Malonyl-CoA:acyl-carrier protein transacylase (MCAT; FabD) from S. aureus has been cloned, overexpressed, purified and crystallized. The crystal belonged to space group P21, with unit-cell parameters a = 41.608, b = 86.717, c = 43.163 Å, α = γ = 90, β = 106.330°, and data were collected to 1.2 Å resolution using synchrotron radiation.
NADH:rubredoxin oxidoreductase from C. acetobutylicum was expressed in E. coli, purified and crystallized. X-ray diffraction data were collected to a resolution of 2.1 Å.
The P. aeruginosa virulence factor Cif, which inhibits cell-surface expression of the cystic fibrosis transmembrane conductance regulator, has been expressed, purified and crystallized.
Recombinant human CLEC5A was crystallized in the trigonal space group P31 and X-ray diffraction data were collected to 1.56 Å resolution.
The emergence of drug-resistant bacteria highlights the importance of identifying potential drug targets. Dihydrodipicolinate synthase (DHDPS) is a valid but as yet unexploited antimicrobial target that functions in the biosynthesis of (S)-lysine. In this study, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DHDPS from S. pneumoniae are described....
Diaminopimelate (DAP) epimerase, an enzyme in the lysine-biosynthetic pathway, is a promising target for antibiotic development against pathogenic bacteria. Here, the cloning, expression, purification, crystallization and preliminary diffraction analysis of DAP epimerase from E. coli are reported.
The N domain of p97/VCP was crystallized in complex with the UBX domain of FAF1. X-ray diffraction data were collected to 2.60 Å resolution and the crystals belonged to space group C2221.
α-Galactosidase from S. cerevisiae has been purified and crystallized in glycosylated and deglycosylated states. X-ray diffraction data were collected to 1.95 Å resolution from the deglycosylated form.
The GyrB subunit of DNA gyrase from X. oryzae pv. oryzae was expressed, purified and crystallized. Diffraction data were collected to a resolution of 2.10 Å.
Stenodactylin is a type 2 RIP from the caudex of Adenia stenodactyla. Stenodactylin crystallization and preliminary X-ray diffraction data analysis are reported.
Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from T. onnurineus NA1 has been purified and crystallized at 295 K.
Given the recent rise in antimicrobial resistance, there is an urgent need to identify and characterize new antibiotic drug targets. One such target is dihydrodipicolinate reductase (DHDPR), which is an essential bacterial enzyme that catalyzes the second step in the lysine-biosynthesis pathway. In this paper, the cloning, expression, purification and crystallization of DHDPR from methicillin-resistant...
Interferon-λ1 and the extracellular domain of its receptor IFN-λ1R1 were expressed in insect cells and purified to homogenity. Ligand–receptor complexes of ligands expressed in insect cells and in E. coli were formed, purified by size-exclusion chromatography and crystallized. Preliminary X-ray studies showed that the crystals diffracted to better than 2.2 Å...
To elucidate which RNA polymerase structural state a particular T. thermophilus Gre-family protein (Gfh1) associates with, the T. thermophilus RNAP elongation complex was cocrystallized with Gfh1.
Crystals of S. elodea ATCC 31461 UDP-glucose dehydrogenase (EC 126.96.36.199) were obtained in space groups P622 and P43212 and diffracted to 2.4 and 3.4 Å resolution, respectively.
A C-terminal truncation construct of human PACSIN 1 (1–344) has been purified and crystallized. Diffraction data were collected to 3.0 Å resolution.
This article describes the first successful crystallization of components of eukaryotic ribonucleases P/MRP. Yeast RNase MRP RNA domain P3 was crystallized in a complex with the proteins Pop6 and Pop7; the crystals diffracted to 3.25 Å resolution.
Aminoglycoside-2′′-phosphotransferase-IVa [APH(2′′)-IVa] is an enzyme that is responsible for high-level gentamicin resistance in E. casseliflavus isolates. Three different crystals of wild-type substrate-free APH(2′′)-IVa have been prepared and preliminary X-ray diffraction experiments have been undertaken on all three crystal forms.
Of the four old yellow enzyme homologues found in S. oneidensis, SYE4 is the homologue most implicated in resistance to oxidative stress. SYE4 was recombinantly expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method.
A complex of the measles virus hemagglutinin and the CD46 receptor representing the initial step of the cell infection has been crystallized.
The crystallization and preliminary X-ray diffraction studies of the Skp1–Fbg3 complex are reported. Crystallization by repeated microseeding using selected crystals as a source of microseeds is described.
Using a peptide derived from H5N1, a complex of duck MHC class I molecule (DuMHC I) with duck β2-microglobulin (Duβ2m) was assembled and crystallized. Initial structure analysis indicated that the crystals did not contain the complete DuMHC I complex but instead contained DuMHC I α3-domain and Duβ2m subunits.
Inositol 1,3,4,5,6-pentakisphosphate kinase from A. thaliana has been expressed in E. coli, purified and crystallized and diffraction data have been collected to 2.3 Å resolution. Two heavy-atom crystal derivatives are under study.
Notes for authors.