3Q3X

Crystal structure of the main protease (3C) from human enterovirus B EV93

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Collection date	2007-02-04
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.872600
Spacegroup name	P 1 21 1
Unit cell lengths	39.072, 65.216, 66.355
Unit cell angles	90.00, 90.67, 90.00

Refinement procedure

Resolution	46.524 - 1.900
R-factor	0.1514
Rwork	0.148
R-free	0.21010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1l1n
RMSD bond length	0.012
RMSD bond angle	1.401
Data reduction software	MOSFLM
Data scaling software	SCALA (3.2.19)
Phasing software	PHASER (1.3)
Refinement software	REFMAC (refmac_5.5.0066)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	66.370	46.524	2.000
High resolution limit [Å]	1.900	6.010	1.900
Rmerge	0.127	0.048	0.412
Total number of observations		4304	11837
Number of reflections	26356
<I/σ(I)>	8.7	12.4	1.6
Completeness [%]	99.9	98.5	100
Redundancy	4.4	5	3.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	18% PEG 8K, 0.1M cacodylate, 0.2M magnesium acetate, cryo + 20% glycerol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K