1QOJ

Crystal Structure of E.coli UvrB C-terminal domain, and a model for UvrB-UvrC interaction.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	1999-05-15
Detector	MARRESEARCH
Wavelength(s)	0.8856, 0.9788, 0.9789
Spacegroup name	P 62
Unit cell lengths	84.810, 84.810, 53.190
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 3.000
R-factor	0.3266
Structure solution method	MAD
RMSD bond length	0.006
RMSD bond angle	0.022
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXL-97
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.110
High resolution limit [Å]	3.000	3.000
Rmerge	0.102	0.511
Total number of observations	65208 *
Number of reflections	4450
<I/σ(I)>		2.75
Completeness [%]	100.0	100
Redundancy	3.86	3.71

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7 *	5 *	BY VAPOUR DIFFUSION 3UL PROTEIN SOLUTION: 2MG/ML UVRB DOMAIN, 20MM TRIS-CL PH7.0, 150MM NACL 0.1% NAN3 + 3UL WELL SOLUTION 0.5ML WELL SOLUTION: 35% SAT. AMMONIUM SULPHATE 100MM TRIS-CL PH8.8, 0.1% NAN3, pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	drop		150 (mM)
4	1	drop		0.1 (%)
5	1	reservoir	ammonium sulfate	35 (%sat)
6	1	reservoir	Tris-HCl	100 (mM)
7	1	reservoir		0.1 (%)