1KQB

Structure of Nitroreductase from E. cloacae complex with inhibitor benzoate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	115
Detector technology	IMAGE PLATE
Collection date	2000-12-15
Detector	RIGAKU RAXIS IV
Spacegroup name	P 1 21 1
Unit cell lengths	52.840, 79.310, 96.920
Unit cell angles	90.00, 93.69, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.189 *
Rwork	0.188
R-free	0.21800 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	1.100
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.880
High resolution limit [Å]	1.800	1.800
Rmerge	0.065	0.162
Number of reflections	72079
<I/σ(I)>	20.3	8.3
Completeness [%]	97.5 *	93.5 *
Redundancy	3.74	3.51

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	homopipes, benzoate, PEG 4000, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	4.75 (mg/ml)
2	1	drop	HEPES	10 (mM)	pH7.
3	1	drop		50 (mM)
4	1	reservoir	homopipes	100 (mg/ml)	pH4.8
5	1	reservoir	acetate	25 (mM)
6	1	reservoir	PEG4000	15 (%)