|Home | About | Journals | Submit | Contact Us | Français|
Comparison of the 2.45 Å resolution crystal structure of homotrimeric RipC, a putative citrate lyase β subunit from Y. pestis, with structural homologs reveals conserved RipC residues that are implicated in CoA binding.
The crystal structure at 1.0 Å resolution of the cellulose-binding CBM3b from the major scaffoldin subunit ScaA of A. cellulolyticus is described.
The structure of PurL from T. thermophilus HB8 in complex with an adenine nucleotide is reported at 2.35 Å resolution.
The equine MHC class I molecule was crystallized in complex with β2-microglobulin and a CTL epitope and X-ray diffraction data were collected to 2.3 Å resolution.
The enzymatic activation of human legumain requires both proteolytic cleavage and conformational reordering and is modulated by its substrate as well as cofactors. These biochemical findings are aided by the crystallization and initial crystallographic analysis of legumain.
HisC2 from M. tuberculosis was cloned, overexpressed, purified and crystallized and the crystals were characterized.
The crystallization of recombinant nitrophorin 7 originating from the bloodsucking insect R. prolixus is described. The crystals diffracted to 1.8 Å resolution.
Chicken interferon-γ receptor α chain was crystallized and diffraction data were collected to 2.0 Å resolution.
Human Cockayne syndrome protein A has been cocrystallized with human DNA damage-binding protein 1 and data have been collected to 2.9 Å resolution.
ADP-ribose pyrophosphatase-I, a Nudix enzyme, from T. thermophilus was crystallized for neutron diffraction. Neutron and X-ray diffraction data sets were collected to 2.1 and 1.5 Å resolution, respectively.
The purification and crystallization of the outer membrane decaheme c-type cytochrome OmcA from S. oneidensis MR-1 are reported. The plate-like crystals belonged to the monoclinic space group P21 and diffracted to 3.25 Å resolution.
CbsA from T. neapolitana has been crystallized. Native data were collected to 2.0 Å resolution.
A human enzyme, DHDPSL, which is homologous to bacterial pyruvate-dependent aldolases but of unknown function, has been expressed, purified and crystallized with the use of in situ proteolysis. The crystals diffracted to 2.0 Å resolution and were suitable for structure determination.
Recombinant wild-type l-lactate dehydrogenase from B. subtilis (BsLDH) was cocrystallized with fructose 1,6-bisphosphate and NAD+ and the crystal diffracted to 2.38 Å resolution. The H171C mutant of BsLDH was also crystallized as the apoenzyme and in complex with NAD+ and the crystals diffracted to 2.20 and 2.49 Å, respectively. All crystals belonged to space group...
Recombinant pyridoxine 4-oxidase from M. loti MAFF303099 was crystallized and diffraction data were collected to 2.2 Å resolution.
A. thaliana dynamin-related protein 1A GTPase domain fused with its GTPase effector domain was overexpressed, purified and crystallized in a hexagonal crystal form that diffracted to 3.6 Å resolution.
This study reports the expression, purification, crystallization and preliminary X-ray crystallographic analysis of human lysosomal β-d-galactosidase.
An orthorhombic crystal of an enoyl-(acyl-carrier protein) reductase from V. fischeri was obtained and diffraction data were collected to 2.7 Å resolution.
The head domain of the DNA-repair protein RecN from D. radiodurans, composed of the amino- and carboxy-terminal domains, was crystallized. X-ray diffraction data were collected to 3.0 Å resolution and the crystals belonged to space group P21.
NaD1 is a potent antifungal plant defensin. Here, the crystallization and preliminary X-ray crystallographic analysis of NaD1 are reported in order to obtain insight into the structural basis of its antifungal activity.
The purification and crystallization of the IL-20–IL-20R1–IL-20R2 ternary complex is described. A low-temperature SAD data set was collected using synchrotron radiation, which showed that the crystals belonged to space group P41212 or its enantiomorph P43212 and contained one ternary complex in the asymmetric unit.
NahF is a salicylaldehyde dehydrogenase that is involved in the naphthalene-degradation pathway, converting salicylaldehyde into salicylate. The subcloning, expression, purification and preliminary X-ray diffraction studies at 2.42 Å resolution of P. putida G7 NahF are reported.
The RNA polymerase domain of primase from S. mutans strain UA159 was cloned, overexpressed, purified and crystallized. X-ray diffraction data were collected to a resolution of 1.60 Å.
A DJ-1 homologue protein from A. thaliana (AtDJ-1D) has been crystallized. Diffraction data were collected to 2.05 Å resolution for structure determination by the multiple-wavelength anomalous dispersion (MAD) method.
Apolipoprotein A-IV crystals consisted of a long unit-cell edge (540 Å) with a high mosaic spread, making them intractable for X-ray diffraction analysis. Extreme dehydration in 60% PEG 3350 was utilized as a post-crystallization treatment as well a screening method to significantly sharpen the mosaic spread and increase the overall resolution of diffraction.
The equilibrium relative humidity values for a number of the most commonly used precipitants in macromolecular crystallization have been measured using a humidity-control device and compared with independent values where available. The results will simplify experiments using the device.