5EUG

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	ROTATING ANODE
Source details	BRUKER
Temperature [K]	100
Detector technology	AREA DETECTOR
Collection date	1998-09-15
Detector	BRUKER
Spacegroup name	P 21 21 21
Unit cell lengths	54.400, 59.400, 64.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	99.000 - 1.600
Structure solution method	AB INITIO
RMSD bond length	0.006
RMSD bond angle	0.022
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	1.658
High resolution limit [Å]	1.600	1.600
Rmerge	0.076	0.300
Number of reflections	126877
<I/σ(I)>	11.4	2.1
Completeness [%]	92.4	58
Redundancy	4.9	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5	20 *	drop consists of equal volume of protein and reservoir solutions *

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-HCl	0.1 (M)