The crystal structure of the 27.5 kDa BLES03 protein was determined at 2.5 Å resolution. Despite having an undetectable sequence relationship, the structure adopts a fold similar to that of eukaryotic initiation factor 4E with minor variations.
2,4-Dihydroxy-hepta-2-ene-1,7-dioate aldolase from E. coli C has been purified and crystallized. Diffraction data were collected to 1.6 Å and structure determination by molecular replacement is in progress.
Human RGS10 and Gαi3 have been overexpressed and purified. Their complex has been crystallized (space group P43212 or P41212, unit-cell parameters a = 99.88, b = 99.88, c = 144.59 Å, α = β = γ = 90°) and diffraction data have been collected to 2.5 Å resolution using synchrotron radiation.
Crystals of P. platycephala chintinase/lectin (PPL-2) belong to the orthorhombic space group P212121, with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 Å. The preliminary cystal structure of PPL-2 was solved at a resolution of 1.73 Å by molecular replacement, presenting a correlation coefficient of 0.558 and an R factor of 0.439.
The protein C-phycocyanin, involved in photosynthesis, has been purified from three cyanobacterial species: Spirulina, Phormidium and Lyngbya. These three proteins have been crystallized and characterized using X-ray crystallography.
The expression and crystallization of recombinant E. coli YeaZ protein, which belongs to a family of proteins of unknown function that are conserved in Gram-positive and Gram-negative bacteria, is reported. Phasing of the diffraction data was performed by the MAD method using the anomalous signal of a gadolinium complex, Gd-DOTMA.
Single crystals of the central structure domains from mumps virus F protein have been obtained by the hanging-drop vapour-diffusion method. A diffraction data set has been collected to 2.2 Å resolution.