7AAM

Crystal structure of the F-BAR domain of PSTIPIP1 bound to the CTH domain of the phosphatase LYP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	105
Detector technology	PIXEL
Collection date	2015-12-09
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.99987
Spacegroup name	P 21 21 21
Unit cell lengths	47.996, 72.037, 205.034
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	102.520 - 2.150
R-factor	0.2068
Rwork	0.205
R-free	0.24090
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	7aan
RMSD bond length	0.001
RMSD bond angle	0.324
Data reduction software	XDS (Jan 21, 2020)
Data scaling software	Aimless (0.7.4)
Phasing software	PHENIX (1.18.2_3874)
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	102.520	2.316
High resolution limit [Å]	2.150	2.154
Rmerge	0.397	3.036
Rmeas	0.407
Rpim		0.722
Number of reflections	20328	1016
<I/σ(I)>	8	1.4
Completeness [%]	51.5	13.4
Redundancy	19.1	17.8
CC(1/2)	0.995	0.521

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	298	100 mM Bis-Tris-propane (pH=6.0), 20% (w/v) PEG 3350, 200 mM sodium citrate. LYP-CTH peptide was soaked into preformed crystals of the F-BAR domain of PSTPIP1.