11AD

Structural basis for high-affinity inhibitor binding to lipid kinases PIP4K2A and PIP4K2B

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	2023-05-22
Detector	DECTRIS EIGER X 9M
Wavelength(s)	0.97934
Spacegroup name	P 61 2 2
Unit cell lengths	135.883, 135.883, 94.679
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	32.440 - 2.790
R-factor	0.17259
Rwork	0.169
R-free	0.23368
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.003
RMSD bond angle	1.029
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	REFMAC (5.8.0419)
Refinement software	REFMAC (5.8.0419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	2.900
High resolution limit [Å]	2.790	2.800
Rmerge	0.107
Rmeas	0.110	0.814
Rpim	0.025	0.178
Number of reflections	13316	1281
<I/σ(I)>	12.7
Completeness [%]	99.9
Redundancy	19.4
CC(1/2)	0.996	0.976

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	295	0.2 M Lithium sulfate monohydrate, 0.1 M HEPES pH 7.5, 25% (w/v) Polyethylene glycol 3350