3P0X

Crystal structure of isocitrate lyase from Brucella melitensis, bound to magnesium isocitrate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2010-08-26
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.541780
Spacegroup name	P 21 21 21
Unit cell lengths	76.910, 135.930, 181.790
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.600 - 2.350
R-factor	0.18
Rwork	0.178
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3oq8
RMSD bond length	0.011
RMSD bond angle	1.246
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.600		2.410
High resolution limit [Å]	2.350	10.510	2.350
Rmerge	0.101	0.028	0.563
Number of reflections	79958	996	5817
<I/σ(I)>	12.13	47.7	2
Completeness [%]	99.8	97.6	99.2
Redundancy	3.8		2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	290	Internal tracking number 217292B10. Protein (26 mg/mL) and PACT Screen condition B10: 0.2 M MgCl2, 20% PEG6000, 0.1 M MES pH 6.0, 5 mM isocitrate, VAPOR DIFFUSION, SITTING DROP, temperature 290K