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Updated: Aug 23, 2026
Crystallization of Membrane Proteins in Lipidic Mesophases
Published on: March 28, 2011
Crystallization and preliminary X-ray diffraction studies of the proteolytically engineered C-terminal half of
S Sharma1, T P Singh, K L Bhatia
1Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Abstract:
The glycosylated functional monoferric C-terminal half (C lobe) (M(r) approximately 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 P2(1) with unit-cell dimensions of a = 44.4, b = 152.3, c= 38.8 A and beta = 105.5 degrees. There is one protein molecule of 40 kDa in the asymmetric unit. A data set at 2.8 A has been collected on an imaging-plate scanner.
