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Human D-Phe-Pro-Arg-CH2-alpha-thrombin crystallization and diffraction data.

E Skrzypczak-Jankun·T J Rydel·A Tulinsky·J W Fenton·K G Mann
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Abstract

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.

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Amino Acid Chloromethyl KetonesCrystallizationHumansThrombinX-Ray DiffractionJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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E Skrzypczak-Jankun, T J Rydel, A Tulinsky, J W Fenton, K G Mann. 1989-04-20. Human D-Phe-Pro-Arg-CH2-alpha-thrombin crystallization and diffraction data.. https://doi.org/10.1016/0022-2836(89)90582-2

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