Human D-Phe-Pro-Arg-CH2-alpha-thrombin crystallization and diffraction data.
Human alpha-thrombin, inhibited with the high-affinity irreversible inhibitor D-Phe-Pro-Arg-chloromethylketone, has been crystallized from polyethylene glycol 8000 solutions buffered with 0.1 M-sodium phosphate. The crystals are: orthorhombic, a = 67.9(1) A, b = 87.9(1) A, c = 61.0(1) A, space group P2(1)2(1)2(1) with four molecules per unit cell. This gives a protein fraction of 58% consistent with the excellent X-ray diffraction quality of the crystals. A mercury heavy-atom derivative is being prepared from a thioester analogue of D-Phe-Pro-Arg-CH2-alpha-thrombin in anticipation of a complete crystallographic structure determination.
Skrzypczak-Jankun
E
E
Department of Chemistry, Michigan State University, East Lansing 48824.
Rydel
T J
TJ
Tulinsky
A
A
Fenton
J W
JW
Mann
K G
KG
D000590:Amino Acid Chloromethyl Ketones; D003460:Crystallization; D006801:Humans; D013917:Thrombin; D014961:X-Ray Diffraction
D000590:Amino Acid Chloromethyl Ketones; D013917:Thrombin; C040308:phenylalanyl-prolyl-arginine-chloromethyl ketone