|Home | About | Journals | Submit | Contact Us | Français|
Crystal structures of human tankyrase I in complex with small-molecule inhibitors PJ34 and XAV939 have been determined, both to 2.0 Å. The TNKS1-PJ34 system allows for displacement soaking and, therefore, is an ideal system for structure-based drug design.
The 0.85 Å room-temperature ultrahigh-resolution structure of H/D-exchanged crambin is reported. Preliminary 1.1 Å resolution neutron diffraction data have been collected at the neutron Protein Crystallography Station at LANSCE.
The structures of new crystal forms of M. tuberculosis peptidyl-tRNA hydrolase confirm and provide further elaboration of the functionally relevant plasticity of the enzyme molecule.
The first crystal structure of a pectin methylesterase from an enteropathogen is presented. This enzyme from Y. enterocolitica has biological significance for the evolution of pectin-metabolic pathways within pectinolytic bacteria and related agents of foodborne illness.
A new crystal lattice structure of H. pylori neutrophil-activating protein has been determined. Iron loading causes a series of conformational changes at the ferroxidase centre.
The structure of a thermostable xylanase from T. fusca is reported.
The interleukin-2 tyrosine kinase Src homology 2 domain was crystallized and its structure was solved to 2.35 Å resolution. The structure reveals a domain-swapped dimer that is related to other dimeric SH2 domains solved previously. The cis–trans-prolyl isomerization that is evident from solution studies of Itk SH2 cannot be observed in the crystal structure.
An unusual case of trace amounts of a contaminating protein facilitating formation of a heterotrimeric protein complex.
The N-terminal F-BAR domain of mouse PACSIN 3, which contains 341 amino acids, has been successfully cloned, purified and crystallized.
A recombinant ATP-dependent DNA ligase from the hyperthermophilic anaerobic archaeon Thermococcus sibiricus was expressed in Escherichia coli and purified. Crystals were grown by vapour diffusion using the hanging-drop method.
The C-terminal domain of the bacteriophage T7 fibre protein gp17, consisting of amino acids 371–553, has been crystallized. Diffraction data have been obtained to around 2.0 Å resolution from two different crystal forms. Multiwavelength anomalous dispersion phasing with a mercury derivative is in progress.
Orthorhombic crystals of DtxR from T. acidophilum have been obtained. X-ray data were collected to 1.8 Å resolution using synchrotron radiation.
The preliminary X-ray analysis of LipC12, the first lipase isolated through a metagenomics approach to be crystallized, is reported.
The M. tuberculosis DNA gyrase A C-terminal domain (CTD) was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P212121 and diffraction data were collected to a resolution of 1.55 Å.
The expression, purification and crystallization of a soluble construct of the putative inner membrane protein PelD from P. aeruginosa is described. The crystals diffracted to a resolution of 2.2 Å.
Several DNA and RNA fragments containing tandem AAAAAA repeats, which were synthesized as analogues of the A-rich repeats found in the autoregulatory sequence of PABP mRNA, have been crystallized, suggesting the possibility that the autoregulatory sequence has a specific structure which impedes the binding of PABP.
Baculovirus envelope protein ODV-E66 (67–704) was crystallized; the crystal diffracted to 1.8 Å resolution and belonged to space group P62 or P64, with unit-cell parameters a = b = 113.5, c = 101.5 Å.
Dioscorin from D. japonica was expressed, purified and crystallized using the sitting-drop vapour-diffusion method. The dioscorin crystal diffracted X-rays to 2.11 Å resolution.
B. cereus arylamine N-acetyltransferase 3 was expressed, purified and crystallized. X-ray diffraction data were collected to 2.42 Å resolution and the crystals belonged to the monoclinic space group C121.
S-Ribosylhomocysteinase (LuxS) encoded by the LuxS gene from Streptococcus mutans was solubly expressed in Escherichia coli, purified and crystallized. Diffraction by the crystal extended to 2.4 Å resolution.
Native and selenomethionine-derivatized (SeMet) crystals of Bacillus subtilis YwfE in the presence of ADP, MgCl2 and the dipeptide l-Ala-l-Gln were obtained using the hanging-drop vapour-diffusion method.
Aspartyl aminopeptidase (APP) is a metallopeptidase that catalyzes the hydrolysis of aspartic acid from the N-termini of polypeptide chains. The apeB gene from P. aeruginosa was cloned, the APP enzyme was expressed and crystallized and a preliminary X-ray crystallographic study was performed in order to understand its unique reaction pathway.
An l-amino-acid oxidase from B. jararacussu venom was crystallized and X-ray diffraction data were collected to a maximum resolution of 3.0 Å.
The expression, purification and crystallization of human dipeptidyl peptidase 10, a component of voltage-gated potassium channels, is described.
The coiled-coil domain of the essential DNA-repair protein RecN from D. radiodurans was crystallized. The crystals belonged to space group P21 and diffracted X-rays to 2.04 Å resolution.
Protein E of the respiratory pathogen H. influenzae is a multifunctional adhesin that is involved in bacterial attachment to host epithelium and direct interactions with vitronectin, laminin and plasminogen. The method of crystallization and X-ray data collection for protein E at 1.8 Å is presented.
The nontoxic nonhaemagglutinin of serotype D neurotoxin complex, which is important in proteolytic stability for toxin complex, was expressed in E. coli, and crystallized.
The refolding, purification and crystallization of FrpB from the meningitis pathogen Neisseria meningitidis is described.
CPIP1 from N. tabacum (NtCPIP1) is a plant heat-shock 40-type protein that participates in effector–host interactions during potyviral infections. Whereas crystals of full-length wild-type NtCPIP1 only diffracted to 8.0 Å resolution, diffraction from crystals of a shortened variant lacking the first 127 amino acids extended to 2.4 Å resolution.
A ribokinase gene (rbk) from the anaerobic halothermophilic bacterium Halothermothrix orenii was cloned and overexpressed in Escherichia coli. The recombinant protein (Ho-Rbk) was purified using immobilized metal-ion affinity chromatography and crystals were obtained using the sitting-drop method.
Orotate phosphoribosyltransferase from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg2+.
Notes for authors.