9qvm

Cryo-EM reconstruction of the NEDD1 anchor protein and CDK5RAP2 bound to the gamma-tubulin ring complex

Method: ELECTRON MICROSCOPY Dmax: 415.5 Å Quality: GOOD

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

Gamma-tubulin complex component 3

Homo sapiens

UniProt Q96CW5

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain B; UniProt 1–907 Chain D; UniProt 1–907 Chain F; UniProt 1–907 Chain H; UniProt 1–907 Chain N; UniProt 1–907 Chain r; UniProt 1–907 Chain s; UniProt 1–907 Chain t; UniProt 1–907 Chain u; UniProt 1–907 Chain v; UniProt 1–907 Not recorded Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–907; UniProt 1–907 Author chain D; PDBConstruct 1–907; UniProt 1–907 Author chain F; PDBConstruct 1–907; UniProt 1–907 Author chain H; PDBConstruct 1–907; UniProt 1–907 Author chain N; PDBConstruct 1–907; UniProt 1–907 Author chain r; PDBConstruct 1–907; UniProt 1–907 Author chain s; PDBConstruct 1–907; UniProt 1–907 Author chain t; PDBConstruct 1–907; UniProt 1–907 Author chain u; PDBConstruct 1–907; UniProt 1–907 Author chain v; PDBConstruct 1–907; UniProt 1–907

Mitotic-spindle organizing protein 1

Homo sapiens

UniProt Q08AG7

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain O; UniProt 1–82 Chain P; UniProt 1–82 Chain Q; UniProt 1–82 Chain R; UniProt 1–82 Chain S; UniProt 1–82 Chain T; UniProt 1–82 Chain U; UniProt 1–82 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

26 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MZT1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain O; PDBConstruct 1–82; UniProt 1–82 Author chain P; PDBConstruct 1–82; UniProt 1–82 Author chain Q; PDBConstruct 1–82; UniProt 1–82 Author chain R; PDBConstruct 1–82; UniProt 1–82 Author chain S; PDBConstruct 1–82; UniProt 1–82 Author chain T; PDBConstruct 1–82; UniProt 1–82 Author chain U; PDBConstruct 1–82; UniProt 1–82

Protein NEDD1

Homo sapiens

UniProt Q8NHV4

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain V; UniProt 1–660 Chain W; UniProt 1–660 Chain X; UniProt 1–660 Chain Y; UniProt 1–660 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEDD1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain V; PDBConstruct 1–660; UniProt 1–660 Author chain W; PDBConstruct 1–660; UniProt 1–660 Author chain X; PDBConstruct 1–660; UniProt 1–660 Author chain Y; PDBConstruct 1–660; UniProt 1–660

Actin, cytoplasmic 1, N-terminally processed

Homo sapiens

UniProt P60709

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain Z; UniProt 1–375 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain Z; PDBConstruct 1–375; UniProt 1–375

Tubulin gamma-1 chain

Homo sapiens

UniProt P23258

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain a; UniProt 1–451 Chain b; UniProt 1–451 Chain c; UniProt 1–451 Chain d; UniProt 1–451 Chain e; UniProt 1–451 Chain f; UniProt 1–451 Chain g; UniProt 1–451 Chain h; UniProt 1–451 Chain i; UniProt 1–451 Chain j; UniProt 1–451 Chain k; UniProt 1–451 Chain l; UniProt 1–451 Chain m; UniProt 1–451 Chain n; UniProt 1–451 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

31 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBG1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain a; PDBConstruct 1–451; UniProt 1–451 Author chain b; PDBConstruct 1–451; UniProt 1–451 Author chain c; PDBConstruct 1–451; UniProt 1–451 Author chain d; PDBConstruct 1–451; UniProt 1–451 Author chain e; PDBConstruct 1–451; UniProt 1–451 Author chain f; PDBConstruct 1–451; UniProt 1–451 Author chain g; PDBConstruct 1–451; UniProt 1–451 Author chain h; PDBConstruct 1–451; UniProt 1–451 Author chain i; PDBConstruct 1–451; UniProt 1–451 Author chain j; PDBConstruct 1–451; UniProt 1–451 Author chain k; PDBConstruct 1–451; UniProt 1–451 Author chain l; PDBConstruct 1–451; UniProt 1–451 Author chain m; PDBConstruct 1–451; UniProt 1–451 Author chain n; PDBConstruct 1–451; UniProt 1–451

Gamma-tubulin complex component 4

Homo sapiens

UniProt Q9UGJ1

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain I; UniProt 1–667 Chain K; UniProt 1–667 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–667; UniProt 1–667 Author chain K; PDBConstruct 1–667; UniProt 1–667

Isoform 3 of Gamma-tubulin complex component 2

Homo sapiens

UniProt Q9BSJ2

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain A; UniProt 1–930 Chain C; UniProt 1–930 Chain E; UniProt 1–930 Chain G; UniProt 1–930 Chain M; UniProt 1–930 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP2_HUMAN
Isoform Q9BSJ2-4
PDB entities 7
Chains and sequence ranges Author chain A; PDBConstruct 1–930; UniProt 1–930 Author chain C; PDBConstruct 1–930; UniProt 1–930 Author chain E; PDBConstruct 1–930; UniProt 1–930 Author chain G; PDBConstruct 1–930; UniProt 1–930 Author chain M; PDBConstruct 1–930; UniProt 1–930

TUBGCP6 protein

Homo sapiens

UniProt B2RWN4

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain L; UniProt 1–1811 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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 B2RWN4_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–1811; UniProt 1–1811

Gamma-tubulin complex component 5

Homo sapiens

UniProt Q96RT8

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain J; UniProt 1–1024 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCP5_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–1024; UniProt 1–1024

Mitotic-spindle organizing protein 2B

Homo sapiens

UniProt Q6NZ67

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain p; UniProt 1–158 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) CDK5 regulatory subunit-associated protein 2 × 2 (A0A0A0MRG9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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 MZT2B_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain p; PDBConstruct 1–158; UniProt 1–158

CDK5 regulatory subunit-associated protein 2

Homo sapiens

UniProt A0A0A0MRG9

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain w; UniProt 1–1663 Chain x; UniProt 1–1663 Not recorded Gamma-tubulin complex component 3 × 10 (Q96CW5) Mitotic-spindle organizing protein 1 × 7 (Q08AG7) Protein NEDD1 × 4 (Q8NHV4) Actin, cytoplasmic 1, N-terminally processed × 1 (P60709) Tubulin gamma-1 chain × 14 (P23258) Gamma-tubulin complex component 4 × 2 (Q9UGJ1) Isoform 3 of Gamma-tubulin complex component 2 × 5 (Q9BSJ2) TUBGCP6 protein × 1 (B2RWN4) Gamma-tubulin complex component 5 × 1 (Q96RT8) Mitotic-spindle organizing protein 2B × 1 (Q6NZ67) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 6.80 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 A0A0A0MRG9_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain w; PDBConstruct 1–1663; UniProt 1–1663 Author chain x; PDBConstruct 1–1663; UniProt 1–1663

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 9qvm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9qvm
Deposition date deposition_date2025-04-11
Structure title titleCryo-EM reconstruction of the NEDD1 anchor protein and CDK5RAP2 bound to the gamma-tubulin ring complex
Keywords keywordsTubulin complex, 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_electron110.10
Forward intensity I(0) i031578500000.00
Molecular weight molecular_weight1244000.0 kDa
Excluded volume excluded_volume1433400 ų
Envelope volume envelope_volume4042500 ų
Hydration-shell volume shell_volume311470 ų
Envelope diameter envelope_diameter325.9
Shell Rg shell_rg110.50
Envelope Rg envelope_rg99.20
Shape Rg shape_rg110.10
Total Rg total_rg110.10
Total atoms total_atoms88888
Residues n_residues17948
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 dmax415.5
Rg (real space) rg_real116.10
Rg uncertainty (real space) rg_real_error3.31
I(0) (real space) i0_real3.1770e+10
I(0) uncertainty (real space) i0_real_error7.4270e+08
Rg (reciprocal space) rg_reciprocal113.90
I(0) (reciprocal space) i0_reciprocal31890000000.0000
Solution quality estimate total_estimate0.8681
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary148.4
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis0.232
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha0.8511
Highest regularization parameter α highest_alpha981300000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.710; Stabil: 0.853; Sysdev: 1.000; Positv: 1.000; Valcen: 0.902; Smooth: 0.718

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (2)

9. Files and Curves (10)