11OP

Crystal Structure of M. tuberculosis ClpP1P2 bound to ONC201

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-1
Synchrotron site	NSLS-II
Beamline	17-ID-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-02-16
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.92010
Spacegroup name	C 1 2 1
Unit cell lengths	210.268, 181.830, 95.133
Unit cell angles	90.00, 94.72, 90.00

Refinement procedure

Resolution	31.590 - 3.110
R-factor	0.1895
Rwork	0.187
R-free	0.24170
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.938
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	3.150
High resolution limit [Å]	3.100	8.400	3.100
Rmerge	0.150	0.031	0.929
Rmeas	0.181	0.037	1.149
Rpim	0.099	0.020	0.665
Number of reflections	62136	3141	3047
<I/σ(I)>	8.66	30.33	1
Completeness [%]	98.2		96.3
Redundancy	3.2		2.7
CC(1/2)	0.987	0.998	0.470

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	1:1 mixture of reservoir (0.1M Bis-Tris (pH 6.5), 15% PEG3350, 0.2M sodium citrate, 10% ethylene glycol) and protein solution (3.75 mg/mL ClpP1, 3.75 mg/mL ClpP2, 0.83 mM ADEP, 0.83 mM Bz-Leu-Leu, 10 mM HEPES (pH 7.5), 50 mM NaCl, 4.5% DMSO)