1F8W

CRYSTAL STRUCTURE OF NADH PEROXIDASE MUTANT: R303M

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	1996-08-08
Detector	MARRESEARCH
Spacegroup name	I 41 2 2
Unit cell lengths	155.180, 155.180, 189.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.450
R-factor	0.196 *
Rwork	0.196
R-free	0.23400
RMSD bond length	0.016
RMSD bond angle	3.000
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000
High resolution limit [Å]	2.450	2.450
Rmerge	0.048 *	0.363
Total number of observations	60231 *
Number of reflections	36615
<I/σ(I)>	9.5	2.6
Completeness [%]	85.8	70.9 *
Redundancy	5.4	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.2	296	2% PEG 400, 2.0 M (NH4)2SO4, 100 mM Na Hepes, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 296K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG400	2-8 (%)
2	1	drop	ammonium sulfate	1.6-1.9 (M)
3	1	drop	sodium HEPES	0.1 (M)
4	1	drop	protein	7.5-10 (mg/ml)