1RR9

Catalytic domain of E.coli Lon protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-24
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 31
Unit cell lengths	86.210, 86.210, 122.680
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 * - 2.100
Rwork	0.243
R-free	0.29600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.300
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.056	0.624 *
Total number of observations	127371 *
Number of reflections	58314
<I/σ(I)>	14.1
Completeness [%]	98.0	99.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	Ammonium sulfate, PIPES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	18 (mg/ml)
2	1	reservoir	ammonium sulfate	2 (M)
3	1	reservoir	PIPES	0.1 (M)	pH6.5