1H69

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,3,5,6,TETRAMETHYL-P-BENZOQUINONE (DUROQUINONE) AT 2.5 ANGSTROM 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	1999-08-15
Detector	BRANDEIS
Spacegroup name	P 1
Unit cell lengths	55.525, 56.912, 97.045
Unit cell angles	77.06, 76.81, 86.86

Refinement procedure

Resolution	32.340 - 1.860
R-factor	0.209 *
Rwork	0.229
R-free	0.25700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ad4
RMSD bond length	0.009
RMSD bond angle	21.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.660
High resolution limit [Å]	0.860 *
Rmerge	0.073
Number of reflections	105655
Completeness [%]	93.7 *	84 *
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *	25 *	Faig, M., (2000) Proc.Natl.Acad.Sci.USA, 97, 3177. *

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)