1H66

CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE CO WITH 2,5-diaziridinyl-3-hydroxyl-6-methyl-1,4-benzoquinone

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
Detector	BRANDEIS CCD
Spacegroup name	P 1
Unit cell lengths	56.185, 57.080, 97.323
Unit cell angles	77.05, 77.07, 87.22

Refinement procedure

Resolution	19.960 - 2.000
R-factor	0.199 *
Rwork	0.256
R-free	0.25600 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	22.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.960
High resolution limit [Å]	2.000
Rmerge	0.091 *
Number of reflections	73718
Completeness [%]	93.8	83.8 *
Redundancy	3.9 *

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)