1D4A

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	1999-09-19
Detector	BRANDEIS - B4
Spacegroup name	P 1
Unit cell lengths	55.678, 57.032, 97.402
Unit cell angles	77.04, 76.72, 86.89

Refinement procedure

Resolution	43.630 - 1.700
R-factor	0.209
Rwork	0.209
R-free	0.25300
RMSD bond length	0.008
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	43.440	1.790
High resolution limit [Å]	1.700	1.700
Rmerge	0.052 *	0.159
Number of reflections	98473 *
<I/σ(I)>	4.9
Completeness [%]	78.8	24.2
Redundancy	3.1	1.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	25 *	30 % PEG 3350 200 MM NAACETATE 12-24 MICROM FAD 100MM NA-TRICINE PH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	Tris-HCl	25 (mM)
3	1	drop	FAD	0.005 (mM)
4	1	reservoir	PEG3350	30 (%)
5	1	reservoir	sodium acetate	200 (mM)
6	1	reservoir	sodium tricine	100 (mg/ml)
7	1	reservoir	FAD	0.012-0.024 (mM)