1VJ1

Crystal structure of putative NADPH-dependent oxidoreductase from Mus musculus at 2.10 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.2
Synchrotron site	ALS
Beamline	8.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2003-05-09
Detector	ADSC
Wavelength(s)	0.97950, 0.9793, 0.9567
Spacegroup name	P 21 21 21
Unit cell lengths	42.386, 91.805, 100.565
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.280 - 2.100
R-factor	0.182
Rwork	0.180
R-free	0.21600
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	1.470 *
Data reduction software	MOSFLM
Data scaling software	SCALA (4.2))
Phasing software	SOLVE
Refinement software	REFMAC (5.1.9999)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.280 *	2.150
High resolution limit [Å]	2.100	2.100
Rmerge	0.069 *	0.431 *
Total number of observations	135157 *
Number of reflections	22433 *
<I/σ(I)>	10.9	1.7
Completeness [%]	95.3	74.9
Redundancy	3.2	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.9 *	277	0.1M Citrate pH 5.1, 0.2M NH4OAc, 15% PEG-4000 , VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K, pH 5.10

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris	20 (mM)	pH7.9
2	1	drop		150 (mM)
3	1	drop	TCEP	0.25 (mM)
4	1	drop	protein	18 (mg/ml)
5	1	reservoir	PEG4000	15 (%)
6	1	reservoir	ammonium acetate	0.2 (M)
7	1	reservoir	sodium citrate	0.1 (M)	pH5.1