SAXSdb — 9yz5

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

Protein adenylyltransferase FICD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 105–433 Chain B； UniProt 105–433	Not recorded	FPP FARNESYL DIPHOSPHATE × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；289 K；100 mM Bis-Tris propane (pH 7.5), 200 mM potassium sodium tartrate, and 21% PEG 3350	Resolution 2.58 Å R-free 0.290

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 9YZ5	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
4U04 Structure of a eukaryotic fic domain containing protein Deposited 2014-07-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Fragment：UNP residues 102-445 Chain B 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	TAR D(-)-TARTARIC ACID × 1 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；289 K；20% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.48 Å R-free 0.245
4U07 ATP bound to eukaryotic FIC domain containing protein Deposited 2014-07-11	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Fragment：UNP residues 102-445 Chain B 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；20% peg 3350, 200mM Na K tartrate, 100mM Bist-Tris Propane 7.5	Resolution 2.64 Å R-free 0.258
4U0S Structure of Eukaryotic fic domain containing protein with ADP Deposited 2014-07-14	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Chain B 102–445（344 aa）	Mutation：E234G Mutation：E234G	ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 PG4 TETRAETHYLENE GLYCOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；20% peg 3350, 200mM Na K tartrate, 100mM Bis-Tris-Propane 7.5	Resolution 2.49 Å R-free 0.245
4U0U Wild type eukaryotic fic domain containing protein with ADP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Fragment：UNP residues 102-445 Chain B 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	PG4 TETRAETHYLENE GLYCOL × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；20% PEG 3350, 200mM Na K tartrate, 100mM Bis-Tris-Propane 7.5	Resolution 2.98 Å R-free 0.256
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Fragment：UNP residues 102-445 Chain G 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain A 102–445（344 aa） Fragment：UNP residues 102-445 Chain G 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain B 102–445（344 aa） Fragment：UNP residues 102-445 Chain H 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain C 102–445（344 aa） Fragment：UNP residues 102-445 Chain E 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain C 102–445（344 aa） Fragment：UNP residues 102-445 Chain E 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 6 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain D 102–445（344 aa） Fragment：UNP residues 102-445 Chain F 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
4U0Z Eukaryotic Fic Domain containing protein with bound APCPP Deposited 2014-07-14	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 7 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: Dimeric	Chain D 102–445（344 aa） Fragment：UNP residues 102-445 Chain F 102–445（344 aa） Fragment：UNP residues 102-445	Not recorded	APC DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER × 2 MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；25% PEG 3350, 200mM Na K Tartrate, 100mM Bis-Tris Propane 7.5	Resolution 2.95 Å R-free 0.251
6I7G Crystal structure of dimeric wild type FICD complexed with ATP Deposited 2018-11-16	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 104–445（342 aa） Chain B 104–445（342 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 2 PEG DI(HYDROXYETHYL)ETHER × 1 1PE PENTAETHYLENE GLYCOL × 2 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M Tris pH 7.5; 20% PEG 300; 5% PEG8K; 10% Glycerol	Resolution 2.70 Å R-free 0.319
6I7H Crystal structure of dimeric FICD mutant K256S Deposited 2018-11-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 104–445（342 aa）	Mutation：K256S	MG MAGNESIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris pH 8.5; 0.05 M Magnesium Chloride; 40% Ethanol	Resolution 2.25 Å R-free 0.259
6I7I Crystal structure of dimeric FICD mutant K256A complexed with MgATP Deposited 2018-11-16	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 104–445（342 aa）	Mutation：K256A	MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M Bis-Tris pH 6.5; 0.2 M Magnesium Chloride; 25% PEG3350	Resolution 2.33 Å R-free 0.325
6I7J Crystal structure of monomeric FICD mutant L258D Deposited 2018-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 104–445（342 aa）	Mutation：L258D	SO4 SULFATE ION × 7 1PE PENTAETHYLENE GLYCOL × 3 PG4 TETRAETHYLENE GLYCOL × 5 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris pH 8.5; 2.0 M Ammonium Sulphate	Resolution 2.65 Å R-free 0.283
6I7K Crystal structure of monomeric FICD mutant L258D complexed with MgATP Deposited 2018-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 104–445（342 aa）	Mutation：L258D	MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 EOH ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；1.0 M Sodium Chloride; 10% Ethanol	Resolution 2.54 Å R-free 0.252
6I7L Crystal structure of monomeric FICD mutant L258D complexed with MgAMP-PNP Deposited 2018-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 104–445（342 aa）	Mutation：L258D	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；1.5 M Sodium Chloride; 10% Ethanol	Resolution 2.32 Å R-free 0.251
6ZMD Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP Deposited 2020-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 102–445（344 aa）	Mutation：T168A, T183A, E234G, L258D, E404C	ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 QMK ~{N}-[2-[1-[(2~{R},3~{R},4~{S},5~{R})-3,4-bis(oxidanyl)-5-[[tris(oxidanyl)-$l^{5}-phosphanyl]oxymethyl]oxolan-2-yl]-1,2,3-triazol-4-yl]ethyl]ethanamide × 1 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；0.2 M NaCl, 0.1 M Na/K phosphate pH 6.2 and 10% (w/v) PEG 8000	Resolution 2.64 Å R-free 0.235
7B7Z DeAMPylation complex of monomeric FICD and AMPylated BiP (state 1) Deposited 2020-12-12	Different construct Different mutation/modification 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 104–445（342 aa）	Mutation：L258D, H363A	AMP ADENOSINE MONOPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；0.1 M MES pH 6.5 10% PEG 4000 0.2 M NaCl	Resolution 1.70 Å R-free 0.221
7B80 DeAMPylation complex of monomeric FICD and AMPylated BiP (state 2) Deposited 2020-12-12	Different construct Different mutation/modification 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 104–445（342 aa）	Not recorded	AMP ADENOSINE MONOPHOSPHATE × 1 MG MAGNESIUM ION × 2 PO4 PHOSPHATE ION × 1 K POTASSIUM ION × 3 P33 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；0.1 M Tris pH 8.0 25% PEG 400	Resolution 1.87 Å R-free 0.228

14 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	FICD_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–330； UniProt 105–433 Author chain B； PDBConstruct 2–330； UniProt 105–433

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	9yz5
Deposition date deposition_date	2025-10-30
Structure title title	human FicD bound with farnesyl pyrophosphate
Keywords keywords	AMPylation, TRANSFERASE; TRANSFERASE
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	30.61 Å
Radius of gyration Rg (electron density) rg_electron	29.76 Å
Forward intensity I(0) i0	92114300.00
Molecular weight molecular_weight	76444.0 kDa
Excluded volume excluded_volume	96090 Å³
Envelope volume envelope_volume	125290 Å³
Hydration-shell volume shell_volume	35164 Å³
Envelope diameter envelope_diameter	96.8 Å
Shell Rg shell_rg	37.10 Å
Envelope Rg envelope_rg	29.02 Å
Shape Rg shape_rg	29.77 Å
Total Rg total_rg	30.44 Å
Total atoms total_atoms	5378
Residues n_residues	658
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	96.4 Å
Rg (real space) rg_real	30.52 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	9.2110e+07
I(0) uncertainty (real space) i0_real_error	1.3470e+06
Rg (reciprocal space) rg_reciprocal	30.56 Å
I(0) (reciprocal space) i0_reciprocal	92120000.0000
Solution quality estimate total_estimate	0.9086
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	94.5 Å
Skewness Skewness skewness	0.176
Kurtosis Kurtosis kurtosis	-0.563
Angular range angular_range	— – 0.2600 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	12500000.0000
Real-space data points n_real_points	53
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.947

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Protein adenylyltransferase FICD
Molecular weight formula_weight	37977.5 kDa
EC 编号 ec_number	2.7.7.108,3.1.4.-
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5462

SEARAALNQALEMKRQGKREKAQKLFMHALKMDPDFVDALTEFGIFSEEDKDIIQADYLYTRALTISPYHEKALVNRDRTLPLVEEIDQRYFSIIDSKVKKVMSIPKGNSALRRVMEETYYHHIYHTVAIGGNTLTLSEIRHILETRYAVPGKSLEEQNEVIGMHAAMKYINTTLVSRIGSVTISDVLEIHRRVLGYVDPVEAGRFRTTQVLVGHHIPPHPQDVEKQMQEFVQWLNSEEAMNLHPVEFAALAHYKLVYIHPFIDGNGRTSRLLMNLILMQAGYPPITIRKEQRSDYYHVLEAANEGDVRPFIRFIAKCTETTLDTLLFAT

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	FARNESYL DIPHOSPHATE
Molecular weight formula_weight	382.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	84

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8. Citations (1)

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Unit-cell length a length_a	71.021 Å
Unit-cell length b length_b	76.983 Å
Unit-cell length c length_c	91.325 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.20 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	monoclinic

Resolution resolution	2.580 Å
Low-resolution limit resolution_low	48.940 Å
R factor r_factor	0.2374
R_work r_work	0.2335
R_free r_free	0.2904

fit	/app/data/saxs_computation/yz/9yz5/9yz5.fit
pddf	/app/data/pr_computation/yz/9yz5/9yz5.pr.out
profile	/app/data/saxs_computation/yz/9yz5/9yz5.dat

human FicD bound with farnesyl pyrophosphate

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

Protein adenylyltransferase FICD

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