3NUB

WbpE, an Aminotransferase from Pseudomonas aeruginosa Involved in O-antigen Assembly in Complex with Product as the External 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	77.924, 148.679, 53.545
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.900 - 1.900
R-factor	0.20159
Rwork	0.199
R-free	0.24298
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3nu7
RMSD bond length	0.009
RMSD bond angle	1.284
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	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.071	0.492
Number of reflections	46379
<I/σ(I)>	36.3	3
Completeness [%]	98.6	100
Redundancy	7.3	6.7

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; Protein incubated with 50 uM PLP and 20 mM UDP-GlcNAc(3NH2)A for 1 hr prior to setting up tray; Drop made by mixing 1.5 uL of protein and reservoir solutions., VAPOR DIFFUSION, HANGING DROP, temperature 298K