6E9P

Crystal structure of tryptophan synthase from M. tuberculosis - open form with BRD0059 bound

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2015-12-17
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97880
Spacegroup name	P 21 21 21
Unit cell lengths	134.660, 157.944, 166.078
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.343 - 2.569
R-factor	0.1766
Rwork	0.176
R-free	0.21700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5tci
RMSD bond length	0.003
RMSD bond angle	0.808
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	HKL-3000
Refinement software	PHENIX (1.12_2829)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	30.000	30.000	2.700
High resolution limit [Å]	2.569	7.160	2.600
Rmerge	0.248	0.121	1.164
Rmeas	0.269	0.131	1.287
Rpim	0.102	0.049	0.535
Number of reflections	110035	5842	5429
<I/σ(I)>	4.4
Completeness [%]	99.9	100	99.4
Redundancy	6.8	7	5.4
CC(1/2)		0.990	0.605

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	289	8% Tacsimate, 20% PEG3350, 5% PEG400