1UI0

Crystal Structure Of Uracil-DNA Glycosylase From Thermus Thermophilus HB8

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL45XU
Synchrotron site	SPring-8
Beamline	BL45XU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-05-23
Detector	RIGAKU RAXIS V
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	45.429, 59.512, 80.971
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.500
R-factor	0.183
Rwork	0.183
R-free	0.20100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Selenomethionyl uracil-DNA glycosylase from Thermus thermophilus HB8
RMSD bond length	0.004
RMSD bond angle	1.180 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.200	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.079 *	0.133 *
Total number of observations	163400 *
Number of reflections	35830
Completeness [%]	99.9	99.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	4 *	1.2-1.5M ammonium sulfate, 75mM Tris, 25% glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14 (mg/ml)
2	1	drop	ammonium sulfate	1.3 (M)
3	1	drop	glycerol	25 (%)
4	1	drop	Tris-HCl	75 (mM)	pH8.5