5X1O

PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSRRC BEAMLINE BL13C1
Synchrotron site	NSRRC
Beamline	BL13C1
Temperature [K]	273
Detector technology	DIFFRACTOMETER
Collection date	2015-12-10
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.975
Spacegroup name	P 21 21 21
Unit cell lengths	34.616, 67.346, 122.196
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.137 - 1.900
R-factor	0.2274
Rwork	0.225
R-free	0.27630
RMSD bond length	0.008
RMSD bond angle	1.219
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	REFMAC
Refinement software	PHENIX ((1.10.1_2155))

Data quality characteristics

	Overall
Low resolution limit [Å]	24.140
High resolution limit [Å]	1.900
Number of reflections	21395
<I/σ(I)>	2.49
Completeness [%]	92.0
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		298	0.1M Sodium citrate, 0.2M Ammonium acetate, 30% PEG 4000