SAXSdb — 9y8v

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Kelch-like protein 12

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 279–567	Not recorded	A1CTF 2-{4-[(1R,2S)-2-{[(3S)-3-(1,1-dioxo-1lambda~6~-thiomorpholin-4-yl)pyrrolidin-1-yl]methyl}cyclopropyl]-2-methyl-1H-1,3-benzimidazol-1-yl}-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.199

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 9Y8V	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2VPJ Crystal structure of the Kelch domain of human KLHL12 Deposited 2008-02-29	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 268–567（300 aa） Fragment：KELCH DOMAIN, RESIDUES 268-567	Not recorded	ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；0.2M AMMONIUM ACETATE, 0.1M SODIUM ACETATE PH4.6, 30% PEG4K	Resolution 1.85 Å R-free 0.222
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	NA SODIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 268–567（300 aa）	Not recorded	NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6TTK Crystal structure of the kelch domain of human KLHL12 in complex with DVL1 peptide Deposited 2019-12-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 268–567（300 aa）	Not recorded	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；30% PEG4000, 0.2 M ammonium acetate, 0.1 M acetate pH 4.6	Resolution 2.38 Å R-free 0.251
6V7O Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex Deposited 2019-12-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；292 K；Sodium cacodylate, Sodium citrate	Resolution 2.90 Å R-free 0.254
6V7O Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex Deposited 2019-12-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；292 K；Sodium cacodylate, Sodium citrate	Resolution 2.90 Å R-free 0.254
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1 NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 268–567（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
8OIO Crystal structure of the kelch domain of human KLHL12 in complex with PLEKHA4 peptide Deposited 2023-03-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 268–567（300 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M citrate pH 5.5, 0.4 M NaCl, 27,1% PEG8K	Resolution 1.95 Å R-free 0.249
8RBH Crystal structure of the kelch domain of human KLHL12 in complex with PEF1 peptide Deposited 2023-12-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 268–567（300 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 1 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M BIS-TRIS pH 5.5, 200 mM NaCl, and 30% PEG4K. (1:1)	Resolution 1.88 Å R-free 0.258
8RBH Crystal structure of the kelch domain of human KLHL12 in complex with PEF1 peptide Deposited 2023-12-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 268–567（300 aa）	Not recorded	NA SODIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；0.1 M BIS-TRIS pH 5.5, 200 mM NaCl, and 30% PEG4K. (1:1)	Resolution 1.88 Å R-free 0.258
9Y8J Crystal structure of the Kelch domain of human KLHL12 with compound 1 Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTS 2-(1H-1,3-benzimidazol-1-yl)-N-(2-fluorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 2.70 Å R-free 0.329
9Y8K Crystal structure of the Kelch domain of human KLHL12 with compound 7k Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTR 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.191
9Y8L Crystal structure of the Kelch domain of human KLHL12 with compound 8e Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTQ 2-(2-amino-5,6-dimethyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.27 Å R-free 0.193
9Y8M Crystal structure of the Kelch domain of human KLHL12 with compound 8i Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTE 2-(2-amino-5-fluoro-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.33 Å R-free 0.178
9Y8N Crystal structure of the Kelch domain of human KLHL12 with compound 8m Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTL 2-(4-methyl-1H-imidazo[4,5-c]pyridin-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.31 Å R-free 0.204
9Y8O Crystal structure of the Kelch domain of human KLHL12 with compound 9c Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTM 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-[2,6-dichloro-4-(phenoxyacetyl)phenyl]acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.29 Å R-free 0.177
9Y8Q Crystal structure of the Kelch domain of human KLHL12 with compound 9e Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTO 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,6-dichloro-4-{[(propan-2-yl)oxy]methyl}phenyl)acetamide × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.20 Å R-free 0.152
9Y8R Crystal structure of the Kelch domain of human KLHL12 with compound 9h Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTP 2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)-N-[2-chloro-4-(hydroxymethyl)-3-methylphenyl]acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.33 Å R-free 0.173
9Y8S Crystal structure of the Kelch domain of human KLHL12 with compound 9k Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTN 4-[2-(2-amino-4-methyl-1H-1,3-benzimidazol-1-yl)acetamido]-N-benzyl-3-chloro-2-methylbenzamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.29 Å R-free 0.170
9Y8T Crystal structure of the Kelch domain of human KLHL12 with compound 10b Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTJ 2-{2-amino-4-[(morpholin-4-yl)methyl]-1H-1,3-benzimidazol-1-yl}-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.40 Å R-free 0.208
9Y8U Crystal structure of the Kelch domain of human KLHL12 with compound 10j Deposited 2025-09-11	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 279–567（289 aa）	Not recorded	A1CTK 2-(4-{[(3S)-3-(4-cyanopiperidin-1-yl)pyrrolidin-1-yl]methyl}-2-methyl-1H-1,3-benzimidazol-1-yl)-N-(2,4,6-trichlorophenyl)acetamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M Bis-Tris pH 5.5, 0.2M MgCl2 and 25% PEG3350	Resolution 1.01 Å R-free 0.141

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	KLH12_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 7–295； UniProt 279–567

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9y8v
Deposition date deposition_date	2025-09-11
Structure title title	Crystal structure of the Kelch domain of human KLHL12 with compound 10q
Keywords keywords	E3 ligase, fragment-based drug discovery, PROTAC, LIGASE; LIGASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	18.60 Å
Radius of gyration Rg (electron density) rg_electron	17.37 Å
Forward intensity I(0) i0	17618100.00
Molecular weight molecular_weight	31355.0 kDa
Excluded volume excluded_volume	38926 Å³
Envelope volume envelope_volume	42322 Å³
Hydration-shell volume shell_volume	19666 Å³
Envelope diameter envelope_diameter	56.4 Å
Shell Rg shell_rg	24.44 Å
Envelope Rg envelope_rg	17.57 Å
Shape Rg shape_rg	17.32 Å
Total Rg total_rg	18.45 Å
Total atoms total_atoms	4314
Residues n_residues	287
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	55.4 Å
Rg (real space) rg_real	18.44 Å
Rg uncertainty (real space) rg_real_error	0.23 Å
I(0) (real space) i0_real	1.7620e+07
I(0) uncertainty (real space) i0_real_error	2.1360e+05
Rg (reciprocal space) rg_reciprocal	18.47 Å
I(0) (reciprocal space) i0_reciprocal	17620000.0000
Solution quality estimate total_estimate	0.9032
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.0 Å
Skewness Skewness skewness	0.021
Kurtosis Kurtosis kurtosis	-0.543
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	7341000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.987

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Kelch-like protein 12
Molecular weight formula_weight	32148.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	4745

GSHMGSANEVLLVVGGFGSQQSPIDVVEKYDPKTQEWSFLPSITRKRRYVASVSLHDRIYVIGGYDGRSRLSSVECLDYTADEDGVWYSVAPMNVRRGLAGATTLGDMIYVSGGFDGSRRHTSMERYDPNIDQWSMLGDMQTAREGAGLVVASGVIYCLGGYDGLNILNSVEKYDPHTGHWTNVTPMATKRSGAGVALLNDHIYVVGGFDGTAHLSSVEAYNIRTDSWTTVTSMTTPRCYVGATVLRGRLYAIAGYDGNSLLSSIECYDPIIDSWEVVTSMGTQRCDAGVCVLRE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	;2-{4-[(1R,2S)-2-{[(3S)-3-(1,1-dioxo-1lambda~6~-thiomorpholin-4-yl)pyrrolidin-1-yl]methyl}cyclopropyl]-2-methyl-1H-1,3-benzimidazol-1-yl}-N-(2,4,6-trichlorophenyl)acetamide ;
Molecular weight formula_weight	625.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	274

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8. Citations (1)

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Unit-cell length a length_a	79.571 Å
Unit-cell length b length_b	79.571 Å
Unit-cell length c length_c	76.631 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	1.271 Å
Low-resolution limit resolution_low	56.329 Å
R factor r_factor	—
R_work r_work	0.1604
R_free r_free	0.1994

fit	/app/data/saxs_computation/y8/9y8v/9y8v.fit
pddf	/app/data/pr_computation/y8/9y8v/9y8v.pr.out
profile	/app/data/saxs_computation/y8/9y8v/9y8v.dat

Crystal structure of the Kelch domain of human KLHL12 with compound 10q

1. Protein Identity and Related Structures Protein Identity & Related Structures

Kelch-like protein 12

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction