3R0O

Crystal structure of carnitinyl-CoA hydratase from Mycobacterium avium

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2010-08-27
Detector	RIGAKU SATURN 944+
Spacegroup name	P 21 21 21
Unit cell lengths	78.890, 105.610, 109.520
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.100
R-factor	0.1718
Rwork	0.169
R-free	0.21630
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3qxi
RMSD bond length	0.014
RMSD bond angle	1.327
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.073	0.024	0.289
Number of reflections	52876	645	3182
<I/σ(I)>	12.78	35.95	2.93
Completeness [%]	97.7	92.4	80.2
Redundancy	3.3		2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5		MyavA.01530.a.A1 PW29034 at 26.76 mg/mL against JCSG+ screen condition D12: 40 mM potassium phosphate monobasic, 15% PEG8000, 20% glycerol, crystal tracking ID 216675d12, pH 7.5, VAPOR DIFFUSION, SITTING DROP