3GKA

Crystal structure of N-ethylmaleimidine reductase from Burkholderia pseudomallei

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2009-02-05
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	49.350, 77.890, 168.940
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.300
R-factor	0.18
Rwork	0.176
R-free	0.23900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2r14
RMSD bond length	0.008
RMSD bond angle	1.068
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.350
High resolution limit [Å]	2.300	2.300
Rmerge	0.134	0.443
Number of reflections	29741
<I/σ(I)>	11.82	3.97
Completeness [%]	99.6	99.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	JCSG+ sparse matrix screen condition H3, 25% PEG3350, 0.1M BisTris pH 5.5, 12.2 mg/mL BupsA00093aB1, crystal ID 200758h3, VAPOR DIFFUSION, SITTING DROP, temperature 289K