4WY2

Crystal structure of universal stress protein E from Proteus mirabilis in complex with UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-N-acetyl-alpha-glucosamine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-24
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 43 21 2
Unit cell lengths	107.877, 107.877, 74.923
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.1736
Rwork	0.172
R-free	0.20180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3olq
RMSD bond length	0.012
RMSD bond angle	1.453
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	HKL-3000
Refinement software	REFMAC (5.8.0073)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.830
High resolution limit [Å]	1.800	4.880	1.800
Rmerge	0.080	0.040	0.892
Rmeas	0.087	0.043	0.976
Rpim	0.033	0.016	0.389
Total number of observations	274114
Number of reflections	41254
<I/σ(I)>	9.5		1.9
Completeness [%]	99.6	98.9	98.7
Redundancy	6.6	6.5	6.1
CC(1/2)		0.999	0.750

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	289	0.2 ul of 12 mg/ml protein in 10mM HEPES, 500mM NaCl pH 7.5 were mixed with 0.2 ul of the Quiagen Cryos Suite condition #50 (1.36 M Ammonium Sulfate, 0.085 M MES pH 6.5, 8.5% Dioxane, 15% Glycerol) and equilibrated against the mother liquor in 96 Well 2 drop Crystallization Plate (MRC)