29VR

Structure of the amyloid-forming peptide YLNSIL from human VIP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-11-23
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.97628
Spacegroup name	P 21 21 21
Unit cell lengths	4.920, 16.960, 45.540
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.770 - 1.150
R-factor	0.0758
Rwork	0.073
R-free	0.10020
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	1.592
Data reduction software	autoPROC
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	22.770	1.170
High resolution limit [Å]	1.150	1.150
Rmeas	0.114	0.592
Number of reflections	1450	34
<I/σ(I)>	12.4
Completeness [%]	89.3
Redundancy	10.8
CC(1/2)	0.998	0.801

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION, RECRYSTALLIZATION		310	the peptide was dissolved at a concentration of 0.4 mg/ml in 30% (v/v) methanol with 0.2 M acetate buffer (pH 3.77) and incubated at 310 K