3Q1T

Crystal structure of enoyl-coA hydratase from Mycobacterium avium

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2010-10-18
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97946
Spacegroup name	P 21 21 2
Unit cell lengths	124.920, 136.890, 104.380
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.350
R-factor	0.191
Rwork	0.189
R-free	0.22730
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1wz8
RMSD bond length	0.014
RMSD bond angle	1.409
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	50.000	2.410
High resolution limit [Å]	2.350	10.510	2.350
Rmerge	0.068	0.018	0.520
Number of reflections	74741
<I/σ(I)>	16.58	49.58	2.82
Completeness [%]	99.4	96.1	99.9
Redundancy	4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	MyavA00829eA1 3C protease cleaved PW28936 at 23.9 mg/mL against JCSG+ screen condition H3, 0.1 M BisTris pH 5.5, 25% PEG 3350 with 25% ethylene glycol as cryo-protectant, crystal tracking ID 216914h3., VAPOR DIFFUSION, SITTING DROP