4EUG

Crystallographic and Enzymatic Studies of an Active Site Variant H187Q of Escherichia Coli Uracil DNA Glycosylase: Crystal Structures of Mutant H187Q and its Uracil Complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	CCD
Collection date	1998-07-15
Detector	BRUKER
Spacegroup name	P 21 21 21
Unit cell lengths	54.100, 59.000, 63.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	99.000 - 1.400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3eug
RMSD bond length	0.010
RMSD bond angle	0.028
Data reduction software	X-GEN
Data scaling software	X-GEN
Phasing software	SHELXS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	1.490
High resolution limit [Å]	1.400	1.400
Rmerge	0.105	0.320
Number of reflections	77493
<I/σ(I)>	18.7	4.5
Completeness [%]	100.0	100
Redundancy	4.4	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	20 *	Xiao, G., (1999) Proteins Struct.Funct.Genet., 35, 13. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	14.9 (mg/ml)
2	1	reservoir	sodium acetate	0.2 (M)
3	1	reservoir	PEG4000	30 (%)
4	1	reservoir	Tris	0.1 (M)