6GQ2

Crystal Structure of the PSMalpha3 Peptide Mutant K12A Forming Cross-Alpha Amyloid-like Fibril

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP		293	Reservoir contained 0.1 M HEPES pH 7.5, 0.5 M Ammonium Sulfate, 30% v/v 2-Methyl-2,4-pentanediol

Crystal Properties
Matthews coefficient	Solvent content
1.64	24.93

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 52.94	α = 90
b = 13.15	β = 112.26
c = 25.97	γ = 90

Symmetry
Space Group	C 1 2 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	PIXEL	DECTRIS EIGER R 4M		2016-11-10	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE MASSIF-3	0.9677	ESRF	MASSIF-3

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	CC (Half)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.54	14.61	94.1	0.114	0.142	0.983	4.83	2.77		2477			24.837

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.54	1.58	91.5		0.836	1.032	0.772	1.2	2.721

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	AB INITIO PHASING	THROUGHOUT	1.54	14.61	2229	248	94.58	0.2067	0.2034	0.236	RANDOM	26.844

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
-3.22		-0.04	-0.7		2.95

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	41.355
r_dihedral_angle_3_deg	13.467
r_sphericity_free	10.969
r_sphericity_bonded	6.633
r_dihedral_angle_1_deg	4.705
r_rigid_bond_restr	2.259
r_angle_refined_deg	1.419
r_angle_other_deg	0.91
r_chiral_restr	0.082
r_bond_refined_d	0.013

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	41.355
r_dihedral_angle_3_deg	13.467
r_sphericity_free	10.969
r_sphericity_bonded	6.633
r_dihedral_angle_1_deg	4.705
r_rigid_bond_restr	2.259
r_angle_refined_deg	1.419
r_angle_other_deg	0.91
r_chiral_restr	0.082
r_bond_refined_d	0.013
r_gen_planes_refined	0.007
r_bond_other_d	0.006
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	181
Nucleic Acid Atoms
Solvent Atoms	3
Heterogen Atoms	5

Software

Software
Software Name	Purpose
XDS	data reduction
XSCALE	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
Arcimboldo	phasing

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.