CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE PROTEOLYTICALLY ENGINEERED C-TERMINAL HALF OF BUFFALO LACTOFERRIN IN ITS IRON-SATURATED FORM

Authors
SHARMA S SINGH TP BHATIA KL
Citation
S. Sharma et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE PROTEOLYTICALLY ENGINEERED C-TERMINAL HALF OF BUFFALO LACTOFERRIN IN ITS IRON-SATURATED FORM, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 116-118
Citations number
22
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
53
Year of publication
1997
Part
1
Pages
116 - 118
Database
ISI
SICI code
0907-4449(1997)53:<116:CAPDSO>2.0.ZU;2-M
Abstract
The glycosylated functional monoferric C-terminal half (C lobe) (M(r) similar or equal to 40 kDa) of buffalo lactoferrin has been produced b y limited proteolysis using proteinase K. The iron-saturated C lobe ha s been crystallized by microdialysis. The crystals belong to the monoc linic system, space group P2(1) with unit-cell dimensions of a=44.4, b =152.3, c=38.8 Angstrom and beta=105.5 degrees. There is one protein m olecule of 40 kDa in the asymmetric unit. A data set at 2.8 Angstrom h as been collected on an imaging-plate scanner.