4O5H

X-ray crystal structure of a putative phenylacetaldehyde dehydrogenase from Burkholderia cenocepacia

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	2013-05-04
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97650
Spacegroup name	C 2 2 21
Unit cell lengths	112.620, 150.070, 345.910
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.1705
Rwork	0.169
R-free	0.19290
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cw3
RMSD bond length	0.013
RMSD bond angle	1.456
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.2)
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.102	0.020	0.482
Number of reflections	195248	2352	14362
<I/σ(I)>	14.62	57.18	3.13
Completeness [%]	99.3	97.8	99.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	0.4 uL protein @ 18 mg/mL + 0.4 uL Morpheus H3 - 10% PEG 4000, 20% glycerol, 0.1 M MES/imidazole pH 6.50, 0.02 M sodium L-glutamate, 0.02 M DL-alanine, 0.02 M glycine, 0.02 M DL-lysine, 0.02 M DL-serine, VAPOR DIFFUSION, SITTING DROP, temperature 289K