SAXSdb — 5cro

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

CRO REPRESSOR PROTEIN

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 B； UniProt 1–66 Chain O； UniProt 1–66	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：microdialysis or batch；pH 7.5；CRYSTALS WERE OBTAINED IN THE PRESENCE OF ABOUT 1.2M PHOSPHATE BY MICRODIALYSIS OR BATCH TECHNIQUES., pH 7.5, microdialysis or batch	Resolution 2.30 Å
2	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–66 Chain C； UniProt 1–66	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：microdialysis or batch；pH 7.5；CRYSTALS WERE OBTAINED IN THE PRESENCE OF ABOUT 1.2M PHOSPHATE BY MICRODIALYSIS OR BATCH TECHNIQUES., pH 7.5, microdialysis or batch	Resolution 2.30 Å
3	Protein homooligomer Homooligomer Protein × 24 PDB declaration: 24-meric（24） Consistent with protein copy count	Chain A； UniProt 1–66 Chain B； UniProt 1–66 Chain C； UniProt 1–66 Chain O； UniProt 1–66	Not recorded	PO4 PHOSPHATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions：microdialysis or batch；pH 7.5；CRYSTALS WERE OBTAINED IN THE PRESENCE OF ABOUT 1.2M PHOSPHATE BY MICRODIALYSIS OR BATCH TECHNIQUES., pH 7.5, microdialysis or batch	Resolution 2.30 Å
4	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–66 Chain B； UniProt 1–66 Chain C； UniProt 1–66 Chain O； UniProt 1–66	Not recorded	PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：microdialysis or batch；pH 7.5；CRYSTALS WERE OBTAINED IN THE PRESENCE OF ABOUT 1.2M PHOSPHATE BY MICRODIALYSIS OR BATCH TECHNIQUES., pH 7.5, microdialysis or batch	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 5CRO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1COP THREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO REPRESSOR IN SOLUTION AS DETERMINED BY HETERONUCLEAR MULTIDIMENSIONAL NMR Deposited 1995-06-23	Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain D 1–66（66 aa） Chain E 1–66（66 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1D1L CRYSTAL STRUCTURE OF CRO-F58W MUTANT Deposited 1999-09-17	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 1–61（61 aa） Fragment：LAMBDA CRO REPRESSOR	Mutation：F58W	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.2 M NH4SO4, 6% isopropanol, including a layer of Hampton's "Al's oil", pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.K	Resolution 2.10 Å R-free 0.258
1D1L CRYSTAL STRUCTURE OF CRO-F58W MUTANT Deposited 1999-09-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–61（61 aa） Fragment：LAMBDA CRO REPRESSOR	Mutation：F58W	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.2 M NH4SO4, 6% isopropanol, including a layer of Hampton's "Al's oil", pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.K	Resolution 2.10 Å R-free 0.258
1D1L CRYSTAL STRUCTURE OF CRO-F58W MUTANT Deposited 1999-09-17	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–61（61 aa） Fragment：LAMBDA CRO REPRESSOR	Mutation：F58W	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2.2 M NH4SO4, 6% isopropanol, including a layer of Hampton's "Al's oil", pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.K	Resolution 2.10 Å R-free 0.258
1D1M CRYSTAL STRUCTURE OF CRO K56-[DGEVK]-F58W MUTANT Deposited 1999-09-17	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–60（60 aa） Fragment：LAMBDA CRO REPRESSOR Chain B 1–60（60 aa） Fragment：LAMBDA CRO REPRESSOR	Mutation：K56[DGEVK]-F58W Mutation：K56[DGEVK]-F58W	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；4.8 M SODIUM FORMATE, 0.5% BETA-OCTYLGLUCOSIDE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.05 Å R-free 0.298
1ORC CRO REPRESSOR INSERTION MUTANT K56-[DGEVK] Deposited 1995-10-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–66（66 aa）	Mutation：INS(K56-DGEVK)	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.54 Å
2A63 Solution structure of a stably monomeric mutant of lambda Cro produced by substitutions in the ball-and-socket interface Deposited 2005-07-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–66（66 aa）	Mutation：A33W, F58D, Y26Q	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.3；293 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR measurement conditions pH 6.1；293 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR measurement conditions pH 6.1；298 K；Ionic strength (raw mmCIF value) no salt added；Pressure ambient NMR sample composition 2.5 mM lambda Cro A33W/F58D/Y26Q U-13C, 50mM Na-phosphate, 90% H2O, 10% D2O, 0.01% sodium azide, 1 mM TSP \| 90% H2O/10% D2O NMR sample composition 5 mM lambda Cro A33W/F58D/Y26Q U-15N, 50mM Na-phosphate, 90% H2O, 10% D2O, 0.01% sodium azide, 1 mM TSP \| 90% H2O/10% D2O NMR sample composition 5 mM lambda Cro A33W/F58D/Y26Q unlabelled, 50mM Na-phosphate, 90% H2O, 10% D2O, 0.01% sodium azide, 1 mM TSP \| 90% H2O/10% D2O NMR sample composition 5 mM lambda Cro A33W/F58D/Y26Q U-15N, 50mM Na-phosphate, 100% D2O, 0.01% sodium azide, 1 mM TSP \| 100% D2O	Resolution not provided
2ECS Lambda Cro mutant Q27P/A29S/K32Q at 1.4 A in space group C2 Deposited 2007-02-14	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 1–66（66 aa） Chain B 1–66（66 aa）	Mutation：Q27P, A29S, K32Q Mutation：Q27P, A29S, K32Q	SO4 SULFATE ION × 4 ACT ACETATE ION × 4 CL CHLORIDE ION × 1 LI LITHIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；80% saturated lithium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.40 Å R-free 0.175
2ECS Lambda Cro mutant Q27P/A29S/K32Q at 1.4 A in space group C2 Deposited 2007-02-14	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–66（66 aa） Chain B 1–66（66 aa）	Mutation：Q27P, A29S, K32Q Mutation：Q27P, A29S, K32Q	SO4 SULFATE ION × 8 ACT ACETATE ION × 8 CL CHLORIDE ION × 2 LI LITHIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；80% saturated lithium sulfate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.40 Å R-free 0.175
2ORC CRO REPRESSOR INSERTION MUTANT K56-[DGEVK], NMR, 32 STRUCTURES Deposited 1998-01-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–66（66 aa）	Mutation：INS(K56-DGEVK)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.6；298 K	Resolution not provided
2OVG Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221 Deposited 2007-02-13	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 1–66（66 aa）	Mutation：Q27P, A29S, K32Q	SO4 SULFATE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M lithium sulfate, 0.1 M Na Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.35 Å R-free 0.171
2OVG Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221 Deposited 2007-02-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–66（66 aa）	Mutation：Q27P, A29S, K32Q	SO4 SULFATE ION × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M lithium sulfate, 0.1 M Na Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.35 Å R-free 0.171
2OVG Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221 Deposited 2007-02-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–66（66 aa）	Mutation：Q27P, A29S, K32Q	SO4 SULFATE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；1.5 M lithium sulfate, 0.1 M Na Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.35 Å R-free 0.171
3ORC CRYSTAL STRUCTURE OF AN ENGINEERED CRO MONOMER BOUND NONSPECIFICALLY TO DNA Deposited 1998-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 2–61（60 aa）	Mutation：INSERTION (K56-DGEVK)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；COCRYSTALS WERE OBTAINED BY MIXING A 1.5 MOLAR EXCESS OF THE 7BP DNA FRAGMENT WITH CRO K56-[DGEVK], COMBINING WITH AN EQUAL VOLUME OF PRECIPITANT BUFFER (140MM AMMONIUM ACETATE, 31% PEG 3350, 100MM ACETATE BUFFER PH 4.6), THEN EQUILIBRATING AGAINST THE PRECIPITANT BUFFER VIA THE HANGING-DROP METHOD AT ROOM TEMPERATURE., vapor diffusion - hanging drop, temperature 293K	Resolution 3.00 Å
4CRO PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX Deposited 1992-01-15	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain A 1–66（66 aa） Chain B 1–66（66 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.9；NA CACODYLATE, NACL, pH 6.90, VAPOR DIFFUSION	Resolution 3.90 Å
4CRO PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX Deposited 1992-01-15	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain C 1–66（66 aa） Chain D 1–66（66 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.9；NA CACODYLATE, NACL, pH 6.90, VAPOR DIFFUSION	Resolution 3.90 Å
4CRO PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX Deposited 1992-01-15	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric	Chain E 1–66（66 aa） Chain F 1–66（66 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.9；NA CACODYLATE, NACL, pH 6.90, VAPOR DIFFUSION	Resolution 3.90 Å
6CRO CRYSTAL STRUCTURE OF LAMBDA-CRO BOUND TO A CONSENSUS OPERATOR AT 3.0 ANGSTROM RESOLUTION Deposited 1998-04-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: hexameric	Chain A 2–61（60 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；CRO PROTEIN WAS SUSPENDED IN 20MM SODIUM CACODYLATE PH6.9 THEN MIXED WITH A 30% EXCESS OF THE 19BP DNA FRAGMENT. THE COMPLEX WAS THEN MIXED WITH AN EQUAL VOLUME OF PRECIPITANT SOLUTION (70MM AMMONIUM SULFATE, 13% PEG3350) AND ALLOWED TO EQUILIBRATE VIA THE HANGING DROP METHOD AT ROOM TEMPERATURE. COCRYSTALS TYPICALLY TAKE 3-4 MONTHS TO APPEAR., vapor diffusion - hanging drop, temperature 293K	Resolution 3.00 Å

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	RCRO_LAMBD
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–66； UniProt 1–66 Author chain B； PDBConstruct 1–66； UniProt 1–66 Author chain C； PDBConstruct 1–66； UniProt 1–66 Author chain O； PDBConstruct 1–66； UniProt 1–66

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	5cro
Deposition date deposition_date	1998-04-17
Structure title title	REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA
Keywords keywords	GENE REGULATING PROTEIN, TRANSCRIPTION REGULATION; GENE REGULATING 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	20.32 Å
Radius of gyration Rg (electron density) rg_electron	19.22 Å
Forward intensity I(0) i0	13122600.00
Molecular weight molecular_weight	27135.0 kDa
Excluded volume excluded_volume	34127 Å³
Envelope volume envelope_volume	41001 Å³
Hydration-shell volume shell_volume	18281 Å³
Envelope diameter envelope_diameter	65.3 Å
Shell Rg shell_rg	24.95 Å
Envelope Rg envelope_rg	19.41 Å
Shape Rg shape_rg	19.19 Å
Total Rg total_rg	20.19 Å
Total atoms total_atoms	1907
Residues n_residues	243
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	64.7 Å
Rg (real space) rg_real	20.26 Å
Rg uncertainty (real space) rg_real_error	0.48 Å
I(0) (real space) i0_real	1.3120e+07
I(0) uncertainty (real space) i0_real_error	1.7650e+05
Rg (reciprocal space) rg_reciprocal	20.27 Å
I(0) (reciprocal space) i0_reciprocal	13120000.0000
Solution quality estimate total_estimate	0.8083
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	26.8 Å
Skewness Skewness skewness	0.216
Kurtosis Kurtosis kurtosis	-0.447
Angular range angular_range	— – 0.3900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4922000.0000
Real-space data points n_real_points	71
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.836; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d5croa_
Class class	a — All alpha proteins
Fold Fold fold	a.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamily	a.35.1 — lambda repressor-like DNA-binding domains
Family Family family	a.35.1.2 — Phage repressors

Domain ID domain_id	d5crob_
Class class	a — All alpha proteins
Fold Fold fold	a.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamily	a.35.1 — lambda repressor-like DNA-binding domains
Family Family family	a.35.1.2 — Phage repressors

Domain ID domain_id	d5croc_
Class class	a — All alpha proteins
Fold Fold fold	a.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamily	a.35.1 — lambda repressor-like DNA-binding domains
Family Family family	a.35.1.2 — Phage repressors

Domain ID domain_id	d5croo_
Class class	a — All alpha proteins
Fold Fold fold	a.35 — lambda repressor-like DNA-binding domains
Superfamily Superfamily superfamily	a.35.1 — lambda repressor-like DNA-binding domains
Family Family family	a.35.1.2 — Phage repressors

CATH v4.4 (4 domains)

Domain ID domain_id	5croA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	240 — CRO Repressor
Homologous superfamily homologous superfamily	10 — CRO Repressor

Domain ID domain_id	5croB00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	240 — CRO Repressor
Homologous superfamily homologous superfamily	10 — CRO Repressor

Domain ID domain_id	5croC00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	240 — CRO Repressor
Homologous superfamily homologous superfamily	10 — CRO Repressor

Domain ID domain_id	5croO00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	240 — CRO Repressor
Homologous superfamily homologous superfamily	10 — CRO Repressor

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8. Citations (19)

Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticity.

J.Mol.Biol. (1998)

PMID: 9653036 · DOI: 10.1006/jmbi.1998.1849 PRIMARY

Different Interactions Used by Cro Repressor in Specific and Nonspecific DNA Binding

J.Biol.Chem. (1986)

Use of Protein Sequence and Structure to Infer Distant Evolutionary Relationships

Chem.Scr. (1986)

The Structure of Cro Repressor Protein

Biological Macromolecules and Assemblies. V.2: Nucleic Acids and Interactive Proteins (1985)

Cro Repressor Protein and its Interaction with DNA

Cold Spring Harbor Symp.Quant.Biol. (1983)

Many Gene-Regulatory Proteins Appear to Have a Similar Alpha-Helical Fold that Binds DNA and Evolved from a Common Precursor

J.Mol.Evol. (1983)

High Resolution Structural Studies of Cro Repressor Protein and Implications for DNA Recognition

J.Biomol.Struct.Dyn. (1983)

DNA-Binding Proteins

Science (1983)

Comparison of the Structures of Cro and Lambda Repressor Proteins from Bacteriophage Lambda

J.Mol.Biol. (1983)

Crystallographic Data for Complexes of the Cro Repressor with DNA

J.Mol.Biol. (1983)

Structural Studies of Protein-Nucleic Acid Interactions

Annu.Rev.Biophys.Bioeng. (1983)

How Does Cro Repressor Recognize its DNA Target Sites?

Trends Biochem.Sci. (1983)

The Molecular Basis of DNA-Protein Recognition Inferred from the Structure of Cro Repressor

Nature (1982)

Structural Similarity in the DNA-Binding Domains of Catabolite Gene Activator and Cro Repressor Proteins

Proc.Natl.Acad.Sci.USA (1982)

Structure of the DNA-Binding Region of Lac Repressor Inferred from its Homology with Cro Repressor

Proc.Natl.Acad.Sci.USA (1982)

Proposed Alpha-Helical Super-Secondary Structure Associated with Protein-DNA Recognition

J.Mol.Biol. (1982)

Structure of the Cro Repressor from Bacteriophage Lambda and its Interaction with DNA

Nature (1981)

The Structure of a Repressor. Crystallographic Data for the Cro Regulatory Protein of Bacteriophage Lambda

J.Mol.Biol. (1979)

Amino Acid Sequence of Cro Regulatory Protein of Bacteriophage Lambda

Nature (1977)

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Unit-cell length a length_a	91.600 Å
Unit-cell length b length_b	91.600 Å
Unit-cell length c length_c	268.500 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	72

Space group space_group	H 3 2
Space-group number int_tables_number	155
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	—
R_work r_work	0.1930
R_free r_free	—

Description description	CRO REPRESSOR PROTEIN
Molecular weight formula_weight	7375.5 kDa
Source method src_method	nat
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	O,A,B,C
Atom count atom_count	1940

REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA

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

CRO REPRESSOR PROTEIN

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

8. Citations (19)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	33

fit	/app/data/saxs_computation/cr/5cro/5cro.fit
pddf	/app/data/pr_computation/cr/5cro/5cro.pr.out
profile	/app/data/saxs_computation/cr/5cro/5cro.dat