1UMN

Crystal structure of Dps-like peroxide resistance protein (Dpr) from Streptococcus suis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ELETTRA BEAMLINE 5.2R
Synchrotron site	ELETTRA
Beamline	5.2R
Temperature [K]	100
Detector technology	CCD
Collection date	2002-02-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	104.735, 138.168, 142.707
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	18.080 - 1.950
R-factor	0.185
Rwork	0.185
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1qgh
RMSD bond length	0.009
RMSD bond angle	1.200
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.010
High resolution limit [Å]	1.950	1.950
Rmerge	0.056	0.272
Number of reflections	146502
<I/σ(I)>	12	1.7
Completeness [%]	97.7	91.3
Redundancy	6.3	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.4	289	HANGING DROP METHOD 2.0 UL 10 MG/ML PROTEIN + 2.0 UL RESERVOUR SOLUTION 27 % PEG 400, 0.2 M CACL2, 0.1M HEPES-NAOH, PH 7.4 +16C FEW DAYS