2BKJ

NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI COMPLEXED WITH NAD+

Experimental procedure

Temperature [K]	287
Detector technology	DIFFRACTOMETER
Collection date	1993-10-10
Detector	ENRAF-NONIUS FAST
Spacegroup name	P 1 21 1
Unit cell lengths	51.200, 85.900, 59.200
Unit cell angles	90.00, 114.70, 90.00

Refinement procedure

Resolution	32.000 - 2.080
R-factor	0.185
Rwork	0.185
R-free	0.20600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bkj
RMSD bond length	0.005
RMSD bond angle	22.700 *
Data reduction software	MADNES
Data scaling software	XSCALE
Phasing software	AMoRE
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.000	2.200
High resolution limit [Å]	2.080	2.080
Rmerge	0.034 *
Number of reflections	23598
Completeness [%]	84.0	38
Redundancy	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7	20 *	Tanner, J., (1994) J.Mol.Biol., 241, 283. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	5-8 (mg/ml)
2	1	drop	Tris-HCl	10 (mM)
3	1	reservoir	PEG6000	30 (%)
4	1	reservoir	HEPES	0.1 (M)