Preliminary crystallographic analyses of the N-terminal lobe of recombinant human serum transferrin.
The N-terminal lobe of recombinant human serum transferrin (residues 1 to 337) has been crystallized in a form suitable for high-resolution three-dimensional X-ray crystallographic analyses. Crystals are of the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 44.9 A, b = 57.0 A and c = 135.9 A, and diffract to beyond 2 A resolution. Further studies show that isomorphous crystals of specifically designed mutants of this protein can also be grown. Structural studies of both recombinant and mutant protein forms will provide a basis for understanding the mechanism by which human serum transferrin functions.
Wang
Y
Y
Department of Biochemistry, University of British Columbia, Vancouver, Canada.
Chen
J
J
Luo
Y
Y
Funk
W D
WD
Mason
A B
AB
Woodworth
R C
RC
MacGillivray
R T
RT
Brayer
G D
GD
D003460:Crystallization; D006801:Humans; D011994:Recombinant Proteins / Q000737:chemistry; D014168:Transferrin / Q000737:chemistry*
D011994:Recombinant Proteins; D014168:Transferrin