9ya1

Cryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat)

Method: ELECTRON MICROSCOPY Dmax: 337.5 Å Quality: GOOD

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

ICMAP4, TGME49_225340

OrganismNot specified

UniProt A0A086KM91

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain 1; UniProt 1–2041 Chain 2; UniProt 1–2041 Not recorded Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A086KM91_TOXGO
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–2041; UniProt 1–2041 Author chain 2; PDBConstruct 1–2041; UniProt 1–2041

Microtubule associated protein SPM1

OrganismNot specified

UniProt A0A7J6K285

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain A; UniProt 1–351 Chain B; UniProt 1–351 Chain C; UniProt 1–351 Chain D; UniProt 1–351 Chain E; UniProt 1–351 Chain F; UniProt 1–351 Chain G; UniProt 1–351 Chain H; UniProt 1–351 Chain I; UniProt 1–351 Chain J; UniProt 1–351 Chain K; UniProt 1–351 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7J6K285_TOXGO
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–351; UniProt 1–351 Author chain B; PDBConstruct 1–351; UniProt 1–351 Author chain C; PDBConstruct 1–351; UniProt 1–351 Author chain D; PDBConstruct 1–351; UniProt 1–351 Author chain E; PDBConstruct 1–351; UniProt 1–351 Author chain F; PDBConstruct 1–351; UniProt 1–351 Author chain G; PDBConstruct 1–351; UniProt 1–351 Author chain H; PDBConstruct 1–351; UniProt 1–351 Author chain I; PDBConstruct 1–351; UniProt 1–351 Author chain J; PDBConstruct 1–351; UniProt 1–351 Author chain K; PDBConstruct 1–351; UniProt 1–351

Tubulin alpha chain

OrganismNot specified

UniProt P10873

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain A0; UniProt 1–453 Chain A2; UniProt 1–453 Chain A4; UniProt 1–453 Chain A6; UniProt 1–453 Chain A8; UniProt 1–453 Chain B0; UniProt 1–453 Chain B2; UniProt 1–453 Chain B4; UniProt 1–453 Chain B6; UniProt 1–453 Chain B8; UniProt 1–453 Chain C0; UniProt 1–453 Chain C2; UniProt 1–453 Chain C4; UniProt 1–453 Chain C6; UniProt 1–453 Chain C8; UniProt 1–453 Chain D0; UniProt 1–453 Chain D2; UniProt 1–453 Chain D4; UniProt 1–453 Chain D6; UniProt 1–453 Chain D8; UniProt 1–453 Chain E0; UniProt 1–453 Chain E2; UniProt 1–453 Chain E4; UniProt 1–453 Chain E6; UniProt 1–453 Chain E8; UniProt 1–453 Chain F0; UniProt 1–453 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA_TOXGO
Isoform
PDB entities 3
Chains and sequence ranges Author chain A0; PDBConstruct 1–453; UniProt 1–453 Author chain A2; PDBConstruct 1–453; UniProt 1–453 Author chain A4; PDBConstruct 1–453; UniProt 1–453 Author chain A6; PDBConstruct 1–453; UniProt 1–453 Author chain A8; PDBConstruct 1–453; UniProt 1–453 Author chain B0; PDBConstruct 1–453; UniProt 1–453 Author chain B2; PDBConstruct 1–453; UniProt 1–453 Author chain B4; PDBConstruct 1–453; UniProt 1–453 Author chain B6; PDBConstruct 1–453; UniProt 1–453 Author chain B8; PDBConstruct 1–453; UniProt 1–453 Author chain C0; PDBConstruct 1–453; UniProt 1–453 Author chain C2; PDBConstruct 1–453; UniProt 1–453 Author chain C4; PDBConstruct 1–453; UniProt 1–453 Author chain C6; PDBConstruct 1–453; UniProt 1–453 Author chain C8; PDBConstruct 1–453; UniProt 1–453 Author chain D0; PDBConstruct 1–453; UniProt 1–453 Author chain D2; PDBConstruct 1–453; UniProt 1–453 Author chain D4; PDBConstruct 1–453; UniProt 1–453 Author chain D6; PDBConstruct 1–453; UniProt 1–453 Author chain D8; PDBConstruct 1–453; UniProt 1–453 Author chain E0; PDBConstruct 1–453; UniProt 1–453 Author chain E2; PDBConstruct 1–453; UniProt 1–453 Author chain E4; PDBConstruct 1–453; UniProt 1–453 Author chain E6; PDBConstruct 1–453; UniProt 1–453 Author chain E8; PDBConstruct 1–453; UniProt 1–453 Author chain F0; PDBConstruct 1–453; UniProt 1–453

Tubulin beta chain

OrganismNot specified

UniProt I7BFC9

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain A1; UniProt 1–449 Chain A3; UniProt 1–449 Chain A5; UniProt 1–449 Chain A7; UniProt 1–449 Chain A9; UniProt 1–449 Chain B1; UniProt 1–449 Chain B3; UniProt 1–449 Chain B5; UniProt 1–449 Chain B7; UniProt 1–449 Chain B9; UniProt 1–449 Chain C1; UniProt 1–449 Chain C3; UniProt 1–449 Chain C5; UniProt 1–449 Chain C7; UniProt 1–449 Chain C9; UniProt 1–449 Chain D1; UniProt 1–449 Chain D3; UniProt 1–449 Chain D5; UniProt 1–449 Chain D7; UniProt 1–449 Chain D9; UniProt 1–449 Chain E1; UniProt 1–449 Chain E3; UniProt 1–449 Chain E5; UniProt 1–449 Chain E7; UniProt 1–449 Chain E9; UniProt 1–449 Chain F1; UniProt 1–449 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I7BFC9_TOXGO
Isoform
PDB entities 4
Chains and sequence ranges Author chain A1; PDBConstruct 1–449; UniProt 1–449 Author chain A3; PDBConstruct 1–449; UniProt 1–449 Author chain A5; PDBConstruct 1–449; UniProt 1–449 Author chain A7; PDBConstruct 1–449; UniProt 1–449 Author chain A9; PDBConstruct 1–449; UniProt 1–449 Author chain B1; PDBConstruct 1–449; UniProt 1–449 Author chain B3; PDBConstruct 1–449; UniProt 1–449 Author chain B5; PDBConstruct 1–449; UniProt 1–449 Author chain B7; PDBConstruct 1–449; UniProt 1–449 Author chain B9; PDBConstruct 1–449; UniProt 1–449 Author chain C1; PDBConstruct 1–449; UniProt 1–449 Author chain C3; PDBConstruct 1–449; UniProt 1–449 Author chain C5; PDBConstruct 1–449; UniProt 1–449 Author chain C7; PDBConstruct 1–449; UniProt 1–449 Author chain C9; PDBConstruct 1–449; UniProt 1–449 Author chain D1; PDBConstruct 1–449; UniProt 1–449 Author chain D3; PDBConstruct 1–449; UniProt 1–449 Author chain D5; PDBConstruct 1–449; UniProt 1–449 Author chain D7; PDBConstruct 1–449; UniProt 1–449 Author chain D9; PDBConstruct 1–449; UniProt 1–449 Author chain E1; PDBConstruct 1–449; UniProt 1–449 Author chain E3; PDBConstruct 1–449; UniProt 1–449 Author chain E5; PDBConstruct 1–449; UniProt 1–449 Author chain E7; PDBConstruct 1–449; UniProt 1–449 Author chain E9; PDBConstruct 1–449; UniProt 1–449 Author chain F1; PDBConstruct 1–449; UniProt 1–449

TLAP3 (apical cap protein AC5), TGME49_235380

OrganismNot specified

UniProt A0A151H4L4

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain O; UniProt 1–583 Chain P; UniProt 1–583 Chain R; UniProt 1–583 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A151H4L4_TOXGO
Isoform
PDB entities 5
Chains and sequence ranges Author chain O; PDBConstruct 1–583; UniProt 1–583 Author chain P; PDBConstruct 1–583; UniProt 1–583 Author chain R; PDBConstruct 1–583; UniProt 1–583

TLAP4 (thioredoxin-like associated protein), TGME49_201760

OrganismNot specified

UniProt A0A7J6K913

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain U; UniProt 1–336 Chain V; UniProt 1–336 Chain W; UniProt 1–336 Chain X; UniProt 1–336 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TRXL1, TGME49_232410 × 22 (Q8MPF4) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7J6K913_TOXGO
Isoform
PDB entities 6
Chains and sequence ranges Author chain U; PDBConstruct 1–336; UniProt 1–336 Author chain V; PDBConstruct 1–336; UniProt 1–336 Author chain W; PDBConstruct 1–336; UniProt 1–336 Author chain X; PDBConstruct 1–336; UniProt 1–336

TRXL1, TGME49_232410

OrganismNot specified

UniProt Q8MPF4

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain a; UniProt 1–220 Chain b; UniProt 1–220 Chain c; UniProt 1–220 Chain d; UniProt 1–220 Chain e; UniProt 1–220 Chain f; UniProt 1–220 Chain g; UniProt 1–220 Chain h; UniProt 1–220 Chain i; UniProt 1–220 Chain j; UniProt 1–220 Chain m; UniProt 1–220 Chain n; UniProt 1–220 Chain o; UniProt 1–220 Chain p; UniProt 1–220 Chain q; UniProt 1–220 Chain r; UniProt 1–220 Chain s; UniProt 1–220 Chain t; UniProt 1–220 Chain u; UniProt 1–220 Chain v; UniProt 1–220 Chain w; UniProt 1–220 Chain x; UniProt 1–220 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL2, TGME49_225790 × 2 (A0A7J6K232) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8MPF4_TOXGO
Isoform
PDB entities 7
Chains and sequence ranges Author chain a; PDBConstruct 1–220; UniProt 1–220 Author chain b; PDBConstruct 1–220; UniProt 1–220 Author chain c; PDBConstruct 1–220; UniProt 1–220 Author chain d; PDBConstruct 1–220; UniProt 1–220 Author chain e; PDBConstruct 1–220; UniProt 1–220 Author chain f; PDBConstruct 1–220; UniProt 1–220 Author chain g; PDBConstruct 1–220; UniProt 1–220 Author chain h; PDBConstruct 1–220; UniProt 1–220 Author chain i; PDBConstruct 1–220; UniProt 1–220 Author chain j; PDBConstruct 1–220; UniProt 1–220 Author chain m; PDBConstruct 1–220; UniProt 1–220 Author chain n; PDBConstruct 1–220; UniProt 1–220 Author chain o; PDBConstruct 1–220; UniProt 1–220 Author chain p; PDBConstruct 1–220; UniProt 1–220 Author chain q; PDBConstruct 1–220; UniProt 1–220 Author chain r; PDBConstruct 1–220; UniProt 1–220 Author chain s; PDBConstruct 1–220; UniProt 1–220 Author chain t; PDBConstruct 1–220; UniProt 1–220 Author chain u; PDBConstruct 1–220; UniProt 1–220 Author chain v; PDBConstruct 1–220; UniProt 1–220 Author chain w; PDBConstruct 1–220; UniProt 1–220 Author chain x; PDBConstruct 1–220; UniProt 1–220

TRXL2, TGME49_225790

OrganismNot specified

UniProt A0A7J6K232

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 heterocomplex Heteromer Protein × 96 PDB declaration: 96-meric(96) Consistent with protein copy count Chain k; UniProt 1–166 Chain l; UniProt 1–166 Not recorded ICMAP4, TGME49_225340 × 2 (A0A086KM91) Microtubule associated protein SPM1 × 11 (A0A7J6K285) Tubulin alpha chain × 26 (P10873) Tubulin beta chain × 26 (I7BFC9) TLAP3 (apical cap protein AC5), TGME49_235380 × 3 (A0A151H4L4) TLAP4 (thioredoxin-like associated protein), TGME49_201760 × 4 (A0A7J6K913) TRXL1, TGME49_232410 × 22 (Q8MPF4) GTP GUANOSINE-5'-TRIPHOSPHATE × 26 MG MAGNESIUM ION × 26 GDP GUANOSINE-5'-DIPHOSPHATE × 26 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.52 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7J6K232_TOXGO
Isoform
PDB entities 8
Chains and sequence ranges Author chain k; PDBConstruct 1–166; UniProt 1–166 Author chain l; PDBConstruct 1–166; UniProt 1–166

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.

SAXS scattering curve SAXS Profile

SAXS profile for 9ya1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ya1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ya1
Deposition date deposition_date2025-09-15
Structure title titleCryo-EM structure of intraconoidal microtubule 2 (ICMT2) from Toxoplasma gondii (8-nm repeat)
Keywords keywords;Tubulin, Microtubule, Microtubule Inner Protein, Microtubule-associated Protein, Toxoplasma gondii, conoid, conoid fiber, intraconoidal microtubule, ICMT, STRUCTURAL PROTEIN ;; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron120.00
Forward intensity I(0) i0147455000000.00
Molecular weight molecular_weight3228200.0 kDa
Excluded volume excluded_volume4009500 ų
Envelope volume envelope_volume7180200 ų
Hydration-shell volume shell_volume478540 ų
Envelope diameter envelope_diameter356.3
Shell Rg shell_rg136.50
Envelope Rg envelope_rg110.00
Shape Rg shape_rg120.00
Total Rg total_rg120.00
Total atoms total_atoms226608
Residues n_residues28687
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax337.5
Rg (real space) rg_real120.80
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.4390e+11
I(0) uncertainty (real space) i0_real_error2.7340e+09
Rg (reciprocal space) rg_reciprocal127.00
I(0) (reciprocal space) i0_reciprocal150600000000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary181.7
Skewness Skewness skewness-0.143
Kurtosis Kurtosis kurtosis-0.715
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha1.7240
Highest regularization parameter α highest_alpha3589000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 0.932; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)