3JST

Crystal structure of transcriptional coactivator/pterin dehydratase from Brucella Melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2009-08-31
Detector	RIGAKU SATURN 944+
Spacegroup name	P 21 21 2
Unit cell lengths	53.759, 85.498, 50.680
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.182
Rwork	0.180
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dch
RMSD bond length	0.006
RMSD bond angle	0.879
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]	85.500	2.140
High resolution limit [Å]	2.100	2.100
Rmerge	0.085	0.233
Number of reflections	14045
<I/σ(I)>	9.4
Completeness [%]	99.1	85.7
Redundancy	6.9	5.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	HAMPTON CRYSTAL SCREEN HT CONDITION G6. 100 MM HEPES PH 7.5, 10% PEG 6000, 5% MPD. PROTEIN CONCENTRATION 23 MG/ML, VAPOR DIFFUSION, SITTING DROP, temperature 293K