1A1R

HCV NS3 PROTEASE DOMAIN:NS4A PEPTIDE COMPLEX

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-07
Detector	RIGAKU RAXIS II
Spacegroup name	H 3 2
Unit cell lengths	225.000, 225.000, 75.450
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	6.000 - 2.500
R-factor	0.216
Rwork	0.216
R-free	0.26100
Structure solution method	MIR
RMSD bond length	0.007
RMSD bond angle	26.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASES
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.590
High resolution limit [Å]	2.500	2.500
Rmerge	0.057	0.355
Number of reflections	24236
<I/σ(I)>	12.4	2.8
Completeness [%]	96.0	91
Redundancy	2.9	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5		PROTEIN WAS CRYSTALLIZED FROM 1.8 M NACL, 100 MM NA/K PHOSPHATE, 10 MM B-MERCAPTOETHANOL, 100 MM MES, PH 6.5.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	MES	0.1 (M)
2	1	reservoir		1.8 (M)
3	1	reservoir	sodium/potassium phosphate	0.1 (M)
4	1	reservoir	beta-mercaptoethanol	10 (mM)