6W2J

CPS1 bound to allosteric inhibitor H3B-374

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X17B1
Synchrotron site	NSLS
Beamline	X17B1
Temperature [K]	120
Detector technology	PIXEL
Collection date	2019-03-14
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	0.9201
Spacegroup name	P 1
Unit cell lengths	71.660, 98.530, 142.530
Unit cell angles	102.13, 97.94, 106.11

Refinement procedure

Resolution	58.960 - 2.620
R-factor	0.1927
Rwork	0.190
R-free	0.25030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6uel
RMSD bond length	0.012
RMSD bond angle	1.561
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	58.960	58.960	2.690
High resolution limit [Å]	2.620	11.720	2.620
Rmerge	0.072	0.019	0.523
Rmeas	0.098	0.025	0.711
Total number of observations	213566
Number of reflections	104121	1142	7718
<I/σ(I)>	9.35	33.08	1.68
Completeness [%]	96.6	94.8	96.3
Redundancy	2.051	2.064	2.113
CC(1/2)	0.996	0.999	0.688

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