3NU8

WbpE, an Aminotransferase from Pseudomonas aeruginosa Involved in O-antigen Assembly in Complex with the Internal Aldimine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X6A
Synchrotron site	NSLS
Beamline	X6A
Temperature [K]	110
Detector technology	CCD
Collection date	2010-02-20
Detector	ADSC QUANTUM 270
Wavelength(s)	0.978
Spacegroup name	P 21 21 2
Unit cell lengths	77.786, 148.723, 53.215
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.830 - 1.500
R-factor	0.19863
Rwork	0.197
R-free	0.22281
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3nu7
RMSD bond length	0.007
RMSD bond angle	1.152
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.091	0.662
Number of reflections	94182
<I/σ(I)>	35.8	3
Completeness [%]	99.7	99.8
Redundancy	7.9	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	298	Crystallization conditions: 0.1 M Bis-Tris, pH 5.5, 0.2 M Ammonium sulfate, 25% PEG 3350 in the reservoir; Protein solution contains 25 mM HEPES, pH 8.0, 100 mM NaCl, 0.5% glycerol; Incubated protein with 50 uM PLP prior to setting up tray; Drop made by mixing 1.5 uL of protein and reservoir solutions., VAPOR DIFFUSION, HANGING DROP, temperature 298K