5J8G

Structure of nitroreductase from E. cloacae complexed with para-nitrobenzoic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-ID-B
Synchrotron site	APS
Beamline	14-ID-B
Temperature [K]	115
Detector technology	CCD
Collection date	2002-10-10
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9
Spacegroup name	P 1 21 1
Unit cell lengths	52.410, 113.440, 82.290
Unit cell angles	90.00, 101.55, 90.00

Refinement procedure

Resolution	19.923 - 1.900
R-factor	0.1696
Rwork	0.166
R-free	0.19720
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	0.538
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	19.923	20.000	1.970
High resolution limit [Å]	1.900	4.080	1.900
Rmerge		0.064	0.270
Rmeas		0.077	0.323
Rpim		0.042	0.176
Completeness [%]		98.4	97.6
Redundancy		3.2	3.2
CC(1/2)		0.990	0.885

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.8	278	100 mM homopipes (pH 4.8), 20 mM para-nitrobenzoic acid, and 13% w/v polyethylene glycol 4000. Protein at 4.75 mg/ml initial concentration in 10 mM HEPES (pH 7.0) and 50 mM KCl