| Literature DB >> 1404372 |
Y Wang1, J Chen, Y Luo, W D Funk, A B Mason, R C Woodworth, R T MacGillivray, G D Brayer.
Abstract
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.Entities:
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Year: 1992 PMID： 1404372 DOI： 10.1016/0022-2836(92)90910-c
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469