1QWL

Structure of Helicobacter pylori catalase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-06-29
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9393
Spacegroup name	P 21 21 2
Unit cell lengths	64.264, 154.502, 95.762
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.000 - 1.600
R-factor	0.18331
Rwork	0.181
R-free	0.21900 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Human erythrocyte catalase
RMSD bond length	0.020
RMSD bond angle	1.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.500	1.690
High resolution limit [Å]	1.600	1.600
Rmerge	0.060 *	0.137 *
Number of reflections	119258 *	7699 *
<I/σ(I)>	13.6
Completeness [%]	94.4	87.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	15% PEG MME 550, 0.1 M sodium citrate, 10 mM ZnSO4, 3 mM NaN3, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	reservoir	PEG550 MME	15 (%)
3	1	reservoir	sodium citrate	0.1 (M)	pH5.6
4	1	reservoir		10 (mM)
5	1	reservoir		3 (mM)