1C5M

STRUCTURAL BASIS FOR SELECTIVITY OF A SMALL MOLECULE, S1-BINDING, SUB-MICROMOLAR INHIBITOR OF UROKINASE TYPE PLASMINOGEN ACTIVATOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1999-03-04
Detector	RIGAKU RAXIS IV++
Spacegroup name	P 31 2 1
Unit cell lengths	81.820, 81.820, 108.790
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	7.500 - 1.950
R-factor	0.226 *
Rwork	0.218
R-free	0.30700
Starting model (for MR)	1fxa
RMSD bond length	0.017 *
RMSD bond angle	3.900
Data reduction software	bioteX ((MSC))
Data scaling software	bioteX
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	70.860	2.040
High resolution limit [Å]	1.640	1.950
Rmerge	0.072	0.265
<I/σ(I)>	6.5	1.6
Completeness [%]	60.0	32.2
Redundancy	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		crystallization conditions : Crystals of truncated human factor Xa were grown in hanging drops from equal volumes of protein solution (5.0 mg/ml in 20 mM Hepes, 50 mM ammonimum sulfate, pH 8.0) and well solution (25 % PEG 5K, 0.10 M Hepes, 0.2 M ammonium sulfate, pH 7.5)., VAPOR DIFFUSION

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.0 (mg/ml)
2	1	drop	HEPES	20 (mM)
3	1	drop	ammonium sulfate	50 (mM)
4	1	reservoir	PEG5000	25 (%)
5	1	reservoir	HEPES	0.10 (M)
6	1	reservoir	ammonium sulfate	0.2 (M)