The crystal structure of the complex of mouse Keap1-DC with a fragment of the nuclear protein prothymosin α was determined and refined to 1.9 Å resolution and revealed that the peptide binds to the bottom region of the β-propeller domain of Keap1-DC.
The crystal structure of the SH3 domain of rat endophilin A2 has been determined by the multiwavelength anomalous dispersion method and refined at a resolution of 1.70 Å to R and Rfree values of 0.196 and 0.217, respectively.
Crystals of the IL-22–sIL-22R1 complex have been obtained by hanging-drop vapor-diffusion experiments combined with streak-seeding at 298 K. A complete low-temperature 3.2 Å resolution data set has been collected using synchrotron radiation.
In order to investigate the role of the protonation states of protein residues in O2 binding, large crystals of deoxy HbA (∼20 mm3) were grown in D2O under anaerobic conditions for neutron diffraction studies.
The cloning, overexpression, purification, crystallization and preliminary X-ray diffraction analysis of a putative peptidoglycan-binding domain of H. pylori MotB, a stator component of the bacterial flagellar motor, are reported.
The cloning, expression, crystallization and preliminary X-ray data analysis of norcoclaurine synthase from T. flavum, a protein which catalyzes the first committed step in the biosynthesis of benzylisoquinoline alkaloids, are reported.
The selenomethionyl-substituted transpeptidase domain of penicillin-binding protein (PBP) 2B from S. pneumoniae was isolated from a limited proteolysis digest of the soluble form of recombinant PBP 2B and then crystallized. MAD data were collected to 2.4 Å resolution.
Seneca Valley Virus-001 of the Picornavirdae family was crystallized in the space group R3 and X-ray diffraction data was collected to a resolution of 2.3 Å. Rotation-function studies suggested the presence of two distict sets of 20 protomers that belong to two different virus particles in the crystallographic asymmetric unit.
Crystals of the complex of the first von Willebrand type C domain (VWC1) of crossveinless 2 (CV2) bound to bone morphogenetic protein 2 (BMP2) exist in two tetragonal crystal forms belonging to either space group P41212 or I41, with one complete BMP2 dimer and two CV2 VWC1 domains per asymmetric unit, and diffract to 2.6 Å resolution.
A recombinant virus-like particle that is a potential oral hepatitis E vaccine was crystallized. Diffraction data were collected to 8.3 Å resolution and the X-ray structure was phased with the aid of a low-resolution density map determined using cryo-electron microscopy data.