Crystallization of the C-terminal domain of rabbit serum hemopexin.
The C-terminal domain of rabbit serum hemopexin, comprising residues 215 to 435, has been crystallized following removal of the attached carbohydrate using the endoglycosidase Endo F. The crystals, grown by vapour diffusion from solutions containing polyethylene glycol 1500, are orthorhombic, with cell dimensions a = 41.0 A, b = 64.2 A, c = 85.2 A, space group P2(1)2(1)2(1), and one molecule in the asymmetric unit. The crystals diffract to 2.4 A resolution and are suitable for X-ray structure analysis.
Baker
H M
HM
Department of Chemistry and Biochemistry, Massey University Palmerston North, New Zealand.
Norris
G E
GE
Morgan
W T
WT
Smith
A
A
Baker
E N
EN
D000818:Animals; D003460:Crystallization; D006466:Hemopexin / Q000737:chemistry*; D011817:Rabbits
D006466:Hemopexin