4EQY

Crystal structure of Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase from Burkholderia thailandensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-12-09
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9774
Spacegroup name	P 1 21 1
Unit cell lengths	109.440, 90.490, 109.520
Unit cell angles	90.00, 111.03, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.1607
Rwork	0.159
R-free	0.18850
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2qiv
RMSD bond length	0.014
RMSD bond angle	1.526
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.051	0.018	0.472
Number of reflections	183552	2104	13526
<I/σ(I)>	18.49	51.94	2.91
Completeness [%]	99.4	95.9	99.1
Redundancy	3.7	3.53	3.76

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5	290	EBS ProPlex screen h7: 15% MPD, 2% PEG4000, 100 mM sodium acetate/HCl pH 5.0, ButhA.00428.a.A1.PS01225 at 32 mg/mL, VAPOR DIFFUSION, SITTING DROP, temperature 290K