4RY1

Crystal structure of periplasmic solute binding protein ECA2210 from Pectobacterium atrosepticum SCRI1043, Target EFI-510858

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-12-05
Detector	RAYONIX MX225HE
Spacegroup name	P 1 21 1
Unit cell lengths	44.751, 93.669, 99.148
Unit cell angles	90.00, 90.19, 90.00

Refinement procedure

Resolution	50.000 - 1.400
R-factor	0.13739
Rwork	0.136
R-free	0.17647
Structure solution method	SAD
RMSD bond length	0.010
RMSD bond angle	1.461
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	SHELX
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.420
High resolution limit [Å]	1.400	1.400
Rmerge	0.104	0.690
Number of reflections	160376
<I/σ(I)>	22.2	2.9
Completeness [%]	99.9	100
Redundancy	7.6	6.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	294	PROTEIN (10 MM HEPES PH 7.5, 5 MM DTT); RESERVOIR: 0.085 M TRIS-HCL, PH 8.5, 0.17 M SODIUM ACETATE, 25% PEG3350, 15% (V/V) GLYCEROL; CRYOPROTECTION: RESERVOIR SOLUTION, VAPOR DIFFUSION, SITTING DROP, temperature 294K