6GQC

Crystal Structure of the PSMalpha3 Peptide Mutant G16A 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 sodium acetate pH 4.6, 0.01 M Cobalt chloride, 1.0 M 1,6-Hexanediol with cryo protection of 20% ethylene glycol

Crystal Properties
Matthews coefficient	Solvent content
1.62	23.84

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 53.27	α = 90
b = 13.3	β = 111.91
c = 25.8	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 PILATUS3 2M		2016-09-17	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID23-2	0.8729	ESRF	ID23-2

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	1.4	14.67	99	0.124	0.135	0.994	8.13	6.302		3478			22.139

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	1.4	1.44	100		0.754	0.822	0.849	2.28	6.131

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	MOLECULAR REPLACEMENT	THROUGHOUT	5I55	1.4	14.67	3129	348	99.29	0.1548	0.1506	0.1928	RANDOM	18.28

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]
-1.54		-0.22	0.95		0.58

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.889
r_dihedral_angle_3_deg	16.501
r_sphericity_free	13.696
r_rigid_bond_restr	6.734
r_sphericity_bonded	4.86
r_dihedral_angle_1_deg	4.316
r_angle_refined_deg	1.385
r_angle_other_deg	0.91
r_chiral_restr	0.086
r_bond_refined_d	0.011

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.889
r_dihedral_angle_3_deg	16.501
r_sphericity_free	13.696
r_rigid_bond_restr	6.734
r_sphericity_bonded	4.86
r_dihedral_angle_1_deg	4.316
r_angle_refined_deg	1.385
r_angle_other_deg	0.91
r_chiral_restr	0.086
r_bond_refined_d	0.011
r_gen_planes_refined	0.008
r_bond_other_d	0.006
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	186
Nucleic Acid Atoms
Solvent Atoms	2
Heterogen Atoms	3

Software

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

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.