1YCP

THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	298
Detector technology	AREA DETECTOR
Detector	SIEMENS
Spacegroup name	P 43 21 2
Unit cell lengths	88.270, 88.270, 195.530
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	7.000 - 2.500
R-factor	0.183
Rwork	0.183
R-free	0.24500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.015
RMSD bond angle	24.580 *
Data reduction software	XENGEN
Data scaling software	XENGEN
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	7.000
High resolution limit [Å]	2.350	2.500 *
Rmerge	0.109
Number of reflections	18614
Completeness [%]	63.0	25 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6 *		2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	peptide	15 (mg/ml)
2	1	drop	ammonium phosphate	0.25 (M)
3	1	reservoir	ammonium sulfate	2 (M)
4	1	reservoir	HEPES	0.1 (M)
5	1	reservoir	PEG400	2 (%)