title: Purification, crystallization, and X-ray diffraction studies of lactotransferrin from buffalo colostrum.
abstract: Lactotransferrin is an iron-binding protein. It has been purified from buffalo colostrum. The purified lactotransferrin has been crystallized in 10% ethanol solution. The crystals are orthorhombic and the space group is P2(1)2(1)2(1) with unit cell dimensions a = 161.70 A, b = 155.75 A, c = 113.48 A. The asymmetric unit contains three molecules of the protein with a solvent content of about 59%. The crystals were stable in the X-ray beam and diffract beyond 3.5 A resolution. The native data have been collected and the structure determination is in progress.
authors.affiliation: Department of Biophysics, All India Institute of Medical Sciences, New Delhi.
authors.forename: A
authors.initials: A
authors.lastname: Raman
authors.forename: K L
authors.initials: KL
authors.lastname: Bhatia
authors.forename: T P
authors.initials: TP
authors.lastname: Singh
authors.forename: A
authors.initials: A
authors.lastname: Srinivasan
authors.forename: C
authors.initials: C
authors.lastname: Betzel
authors.forename: R C
authors.initials: RC
authors.lastname: Malik
mesh_terms: D000818:Animals; D002020:Buffaloes; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003126:Colostrum / Q000737:chemistry*; D003460:Crystallization; D005260:Female; D007781:Lactoferrin / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D007781:Lactoferrin