1O0Q

Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-04-04
Detector	MARRESEARCH
Wavelength(s)	0.98
Spacegroup name	H 3
Unit cell lengths	179.900, 179.900, 37.300
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.200
R-factor	0.191
Rwork	0.189
R-free	0.23700
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.009
RMSD bond angle	1.560
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.900	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.099 *	0.241 *
Total number of observations	81355 *
Number of reflections	22772
Completeness [%]	99.7	99.9
Redundancy	3.6	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	4 *	Villeret, V., (1997) Protein Sci., 6, 2462. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	1.6 (M)
2	1	reservoir	HEPES	0.1 (M)	pH7.0
3	1	drop	protein	15 (mg/ml)