3K5P

Crystal structure of amino acid-binding ACT: D-isomer specific 2-hydroxyacid dehydrogenase catalytic domain 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	2009-10-01
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 62 2 2
Unit cell lengths	97.891, 97.891, 189.215
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.683 - 2.150
R-factor	0.184
Rwork	0.182
R-free	0.21600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2p9c
RMSD bond length	0.014
RMSD bond angle	1.385
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.683	2.230
High resolution limit [Å]	2.150	2.150
Rmerge	0.090	0.554
Number of reflections	29302
<I/σ(I)>	33.2	3.28
Completeness [%]	97.5	82
Redundancy	17.3	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	289	28 mg/mL protein in 25 mM Hepes pH 7, 0.3 M NaCl, 10% glycerol against Cryo Full condition B3: 50% PEG 400, 5% PEG 1000, 10% glycerol, 0.1 M MES pH 6.0, crystal tracking ID 204157b3, VAPOR DIFFUSION, SITTING DROP, temperature 289K