1FXY

COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-ARG-CHLOROMETHYLKETONE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	280
Detector technology	IMAGE PLATE
Collection date	1995-05
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	65.510, 48.920, 75.540
Unit cell angles	90.00, 111.46, 90.00

Refinement procedure

Resolution	8.000 - 2.150
R-factor	0.185 *
Rwork	0.180
R-free	0.24100 *
RMSD bond length	0.005
RMSD bond angle	1.200 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	8.000 *
High resolution limit [Å]	2.150	2.150 *
Rmerge	0.072 *
Total number of observations	28062 *
Number of reflections	10714 *
Completeness [%]	89.3 *	91.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.8	4 *	PROTEIN WAS CRYSTALLIZED FROM 15% PEG 6K, 100 MM HEPES, PH 7.8.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	15 (mg/ml)
2	1	reservoir	HEPES	100 (mM)
3	1	reservoir	PEG6000	15 (%)