Preliminary crystallographic studies on human apo-lactoferrin in its native and deglycosylated forms.
Human apo-lactoferrin in both native and deglycosylated forms has been purified, and crystals obtained by dialysis against low ionic strength buffer solutions. The crystals of native apo-lactoferrin are orthorhombic, space group P2(1)2(1)2(1) with cell dimensions a = 222.0 A, b = 115.6 A, c = 77.8 A and have two protein molecules per asymmetric unit. Two crystal forms of deglycosylated apo-lactoferrin have been obtained. One is orthorhombic, space group P2(1)2(1)2(1), with cell dimensions a = 152.1 A, b = 94.6 A, c = 55.8 A. The second is tetragonal, space group I4, with cell dimensions a = b = 189.4 A, c = 55.1 A. Both of the latter have only one molecule per asymmetric unit, and are suitable for high-resolution X-ray structure analysis.
Norris
G E
GE
Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.
Baker
H M
HM
Baker
E N
EN
D001059:Apoproteins / Q000378:metabolism; D003460:Crystallization; D005947:Glucose / Q000378:metabolism; D006801:Humans; D007781:Lactoferrin / Q000378:metabolism; D007782:Lactoglobulins / Q000378:metabolism; D014961:X-Ray Diffraction
D001059:Apoproteins; D007782:Lactoglobulins; C039223:apolactoferrin; D007781:Lactoferrin; D005947:Glucose