1OOE

Structural Genomics of Caenorhabditis elegans : Dihydropteridine reductase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2002-11-03
Detector	MAR CCD 165 mm
Wavelength(s)	1.07175
Spacegroup name	P 1
Unit cell lengths	41.926, 50.892, 58.770
Unit cell angles	89.98, 71.98, 82.05

Refinement procedure

Resolution	32.280 - 1.650
R-factor	0.201
Rwork	0.194
R-free	0.22700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dhr
RMSD bond length	0.004
RMSD bond angle	1.200
Data scaling software	HKL-2000
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.280 *	1.640
High resolution limit [Å]	1.650 *	1.650 *
Rmerge	0.041 *	0.281 *
Total number of observations	102854 *
Number of reflections	56662
<I/σ(I)>	10	3.1
Completeness [%]	95.3 *	93.8 *
Redundancy	1.9	0.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	295	pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K RESERVOIR: 20% PEG8000, 10 MM MGCL2, 0.1 M AMMONIUM SULFATE, 50 MM MES, PH 5.6; PROTEIN STOCK: 17.3 MG/ML IN 10 MM HEPES, PH 7.0; DROPS: 2 MICROLITERS OF PROTEIN STOCK + 4 MICROLITERS OF RESERVOIR SOLUTION

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	20 (%(w/v))
2	1	reservoir		10 (mM)
3	1	reservoir	ammonium sulfate	0.1 (M)
4	1	reservoir	MES	50 (mM)	pH5.6
5	1	drop	protein	17.3 (mg/ml)
6	1	drop	HEPES	10 (mM)	pH7.