3EOO

2.9A crystal structure of methyl-isocitrate lyase from Burkholderia pseudomallei

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2008-06-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	163.807, 172.404, 179.277
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.000 - 2.900
R-factor	0.24
Rwork	0.237
R-free	0.29900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.522
Data scaling software	d*TREK (9.7L)
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.280	48.280	2.800
High resolution limit [Å]	2.700	5.810	2.700
Rmerge	0.126	0.051	0.534
Total number of observations		69750	64263
Number of reflections	137453
<I/σ(I)>		15.3	2
Completeness [%]	98.6	97	99.2
Redundancy	4.78	4.96	4.64

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	6.5	289	25% PEG 3350, 0.1M BIS-TRIS pH 6.5, 0.2M NaCl, VAPOR DIFFUSION, temperature 289K