1K32

Crystal structure of the tricorn protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2000-12-10
Detector	ADSC QUANTUM 4
Wavelength(s)	0.939
Spacegroup name	P 1 21 1
Unit cell lengths	95.860, 245.998, 159.040
Unit cell angles	90.00, 105.30, 90.00

Refinement procedure

Resolution	20.000 - 2.000
R-factor	0.248 *
Rwork	0.245
R-free	0.25900 *
Structure solution method	MIR+MAD+NCS Averaging
RMSD bond length	0.080 *
RMSD bond angle	1.000 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.050
High resolution limit [Å]	2.000	2.000
Rmerge	0.208 *	0.313
Number of reflections	394093
<I/σ(I)>	6.7	1.9
Completeness [%]	82.8	68.1
Redundancy	2	1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	20 *	25% isopropanol, 0.1 M MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	MES	25-30 (%)	pH6.0