9BT7

Crystal structure of Chorismate Mutase from Mycobacterium tuberculosis in complex with the cyclic peptide inhibitor D1.3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 19-ID
Synchrotron site	NSLS-II
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-02-10
Detector	DECTRIS EIGER2 XE 9M
Wavelength(s)	0.9795
Spacegroup name	P 21 21 21
Unit cell lengths	70.186, 71.102, 71.603
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.950 - 1.800
R-factor	0.1773
Rwork	0.176
R-free	0.20820
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.786
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.20.1_4487: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	71.600	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.204	1.625
Rmeas	0.216	1.720
Rpim	0.069	0.557
Total number of observations	315844	22687
Number of reflections	33927	2458
<I/σ(I)>	8.5	1.4
Completeness [%]	100.0
Redundancy	9.3	9.2
CC(1/2)	0.996	0.636

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.5	291	JCSG+ H7: (25% (w/v) PEG 3350, 0.1 M Bis-Tris pH 5.5, 0.2M Ammonium Sulfate), chorismate mutase at 10 mg/mL. plate 12878, well H7 drop 2. Puck: PSL-0513, Cryo: 80% crystallant and 20% PEG 200 .