Crystallization and preliminary X-ray diffraction studies of the proteolytically engineered C-terminal half of buffalo lactoferrin in its iron-saturated form

The glycosylated functional monoferric C-terminal half (C lobe) (M_r ≃40 kDa) of buffalo lactoferrin has been produced by limited proteolysis using proteinase K. The iron-saturated C lobe has been crystallized by microdialysis. The crystals belong to the monoclinic system, space group P2₁ with unit-cell dimensions of a = 44.4, b = 152.3, c= 38.8 Å and β = 105.5°. There is one protein molecule of 40 kDa in the asymmetric unit. A data set at 2.8 Å has been collected on an imaging-plate scanner.