6IFQ

Crystal structure of a standalone versatile EAL protein from Vibrio cholerae O395 - Apo form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-3
Synchrotron site	ESRF
Beamline	MASSIF-3
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-07-23
Detector	DECTRIS EIGER X 4M
Wavelength(s)	0.9677
Spacegroup name	C 1 2 1
Unit cell lengths	157.701, 42.812, 73.573
Unit cell angles	90.00, 94.61, 90.00

Refinement procedure

Resolution	51.588 - 1.950
R-factor	0.2094
Rwork	0.207
R-free	0.25750
RMSD bond length	0.008
RMSD bond angle	0.950
Data reduction software	XDS
Data scaling software	Aimless (0.3.11)
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	78.590	78.590	2.000
High resolution limit [Å]	1.950	8.940	1.950
Rmerge	0.040	0.031	0.614
Rmeas	0.048	0.040	0.726
Rpim	0.026	0.025	0.383
Total number of observations		1013	8893
Number of reflections	35579	380	2485
<I/σ(I)>	13.4	36.9	1.9
Completeness [%]	98.7	92	99.4
Redundancy	3.5	2.7	3.6
CC(1/2)	0.998	0.996	0.920

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	PEG 4000, sodium citrate, ammonium acetate