3MEP

Crystal Structure of ECA2234 protein from Erwinia carotovora, Northeast Structural Genomics Consortium Target EwR44

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4C
Synchrotron site	NSLS
Beamline	X4C
Temperature [K]	100
Detector technology	CCD
Collection date	2010-02-11
Detector	MAR CCD 165 mm
Wavelength(s)	0.97853
Spacegroup name	C 1 2 1
Unit cell lengths	100.179, 41.930, 148.639
Unit cell angles	90.00, 105.62, 90.00

Refinement procedure

Resolution	36.180 - 2.300
R-factor	0.222
Rwork	0.220
R-free	0.26400
Structure solution method	SAD
RMSD bond length	0.007
RMSD bond angle	1.400
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SHELX (followed by SOLVE/RESOLVE)
Refinement software	CNS (1.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	36.180	2.340
High resolution limit [Å]	2.300	2.300
Rmerge	0.082	0.369
Number of reflections	51199
<I/σ(I)>	17.3	3.05
Completeness [%]	96.5	82.4
Redundancy	2.1	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	291	Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5) . Reservoir solution: 0.1M Hepes (pH 7), 16% PEG 8k, and 0.2M sodium nitrate., VAPOR DIFFUSION, HANGING DROP, temperature 291K