SAXSdb — 1a45

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

GAMMAF CRYSTALLIN

OrganismNot specified

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 1–173	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；pH 7.0	Resolution 2.30 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.

Other PDB	Difference from Current Entry 1A45	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1M8U Crystal Structure of Bovine gamma-E at 1.65 Ang Resolution Deposited 2002-07-26	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–173（173 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 4.5；277 K；PEG 3000, sodium acetate, pH 4.5, microbatch, temperature 277K	Resolution 1.65 Å R-free 0.216

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

View Construct and Data Evidence

UniProt name	CRGF_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–173； UniProt 1–173

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	1a45
Deposition date deposition_date	1998-02-10
Structure title title	GAMMAF CRYSTALLIN FROM BOVINE LENS
Keywords keywords	EYE LENS PROTEIN; EYE LENS PROTEIN
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	18.01 Å
Radius of gyration Rg (electron density) rg_electron	16.88 Å
Forward intensity I(0) i0	9007160.00
Molecular weight molecular_weight	20955.0 kDa
Excluded volume excluded_volume	25617 Å³
Envelope volume envelope_volume	29062 Å³
Hydration-shell volume shell_volume	14927 Å³
Envelope diameter envelope_diameter	59.4 Å
Shell Rg shell_rg	22.27 Å
Envelope Rg envelope_rg	17.07 Å
Shape Rg shape_rg	16.87 Å
Total Rg total_rg	17.75 Å
Total atoms total_atoms	1481
Residues n_residues	173
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	59.8 Å
Rg (real space) rg_real	18.01 Å
Rg uncertainty (real space) rg_real_error	0.37 Å
I(0) (real space) i0_real	9.0070e+06
I(0) uncertainty (real space) i0_real_error	1.0360e+05
Rg (reciprocal space) rg_reciprocal	18.01 Å
I(0) (reciprocal space) i0_reciprocal	9007000.0000
Solution quality estimate total_estimate	0.8727
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	20.2 Å
Skewness Skewness skewness	0.373
Kurtosis Kurtosis kurtosis	-0.273
Angular range angular_range	— – 0.4400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1900000.0000
Real-space data points n_real_points	75
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.800; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.944

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1a45a1
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

Domain ID domain_id	d1a45a2
Class class	b — All beta proteins
Fold Fold fold	b.11 — gamma-Crystallin-like
Superfamily Superfamily superfamily	b.11.1 — gamma-Crystallin-like
Family Family family	b.11.1.1 — Crystallins/Ca-binding development proteins

CATH v4.4 (2 domains)

Domain ID domain_id	1a45A01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

Domain ID domain_id	1a45A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	20 — Gamma-B Crystallin; domain 1
Homologous superfamily homologous superfamily	10 — Crystallins

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8. Citations (5)

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Unit-cell length a length_a	35.100 Å
Unit-cell length b length_b	46.200 Å
Unit-cell length c length_c	186.200 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	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1860
R_work r_work	0.1860
R_free r_free	—

Description description	GAMMAF CRYSTALLIN
Molecular weight formula_weight	20985.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1688

GAMMAF CRYSTALLIN FROM BOVINE LENS

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

GAMMAF CRYSTALLIN

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

8. Citations (5)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	207

fit	/app/data/saxs_computation/a4/1a45/1a45.fit
pddf	/app/data/pr_computation/a4/1a45/1a45.pr.out
profile	/app/data/saxs_computation/a4/1a45/1a45.dat