6UEL

CPS1 bound to allosteric inhibitor H3B-193

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	120
Detector technology	PIXEL
Collection date	2019-06-20
Detector	DECTRIS PILATUS3 6M
Wavelength(s)	1.00
Spacegroup name	P 1 21 1
Unit cell lengths	99.587, 132.342, 142.443
Unit cell angles	90.00, 102.57, 90.00

Refinement procedure

Resolution	139.030 - 1.900
R-factor	0.1739
Rwork	0.172
R-free	0.20860
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5dot
RMSD bond length	0.019
RMSD bond angle	1.841
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	139.030	50.000	1.930
High resolution limit [Å]	1.900	5.160	1.900
Rmerge	0.098	0.050	0.987
Rmeas	0.110	0.055	1.110
Rpim	0.048	0.024	0.499
Number of reflections	281085	14056	14009
<I/σ(I)>	6.2
Completeness [%]	99.3	97.5	99.7
Redundancy	5	5.1	4.8
CC(1/2)		0.993	0.611

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	CPS1 protein was buffer exchanged into 50 mM glycyl-glycine pH 7.4, 50 mM KCl, 5% glycerol. CPS1 was concentrated to 10 mg/ml and H3B-4193 was added to a 5x excess molar ratio along with 1mM AMPPNP and 1mM NAG. Ligand bound complex crystals grew by hanging drop vapor diffusion in 20% PEG 3350 and 0.2M trisodium citrate