2HOB

Crystal structure of SARS-CoV main protease with authentic N and C-termini in complex with a Michael acceptor N3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2006-06-03
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	108.566, 81.210, 53.287
Unit cell angles	90.00, 104.48, 90.00

Refinement procedure

Resolution	50.000 - 1.950
R-factor	0.205
Rwork	0.202
R-free	0.22100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1uk3
RMSD bond length	0.015
RMSD bond angle	1.830
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.020
High resolution limit [Å]	1.950	1.950
Number of reflections	32068
Completeness [%]	99.6	97.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	291	2% polyethylene glycol(PEG) 6000, 3% DMSO, 1mM DTT, 0.1M [2-(N-morpholino)ethanesulfonic acid] (Mes) buffer (pH 6.0), with a protein concentration of 5mg/ml. Inhibitor N3 was dissolved in 7.5% PEG 6000, 6% DMSO, and 0.1M Mes (pH 6.0) with a concentration of 10mM (supersaturation). Then, a 3 micro-l aliquot of such solution was added to the drop, and the crystals were soaked for approximately 2-6 days., VAPOR DIFFUSION, HANGING DROP, temperature 291K