+Open data
-Basic information
Entry | Database: PDB / ID: 8p91 | ||||||
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Title | Hfq from Chromobacterium haemolyticum; a P6 space group monomer | ||||||
Components | RNA-binding protein Hfq | ||||||
Keywords | RNA BINDING PROTEIN / Hfq / translation regulation | ||||||
Function / homology | RNA-binding protein Hfq / Hfq protein / : / Sm domain profile. / LSM domain superfamily / regulation of DNA-templated transcription / RNA binding / RNA-binding protein Hfq Function and homology information | ||||||
Biological species | Chromobacterium haemolyticum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.4 Å | ||||||
Authors | Nikulin, A.D. / Lekontseva, N.V. | ||||||
Funding support | Russian Federation, 1items
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Citation | Journal: Crystallography Reports Title: Hfq from Chromobacterium haemolyticum Authors: Nikulin, A.D. / Lekontseva, N.V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8p91.cif.gz | 30.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8p91.ent.gz | 18 KB | Display | PDB format |
PDBx/mmJSON format | 8p91.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8p91_validation.pdf.gz | 418.6 KB | Display | wwPDB validaton report |
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Full document | 8p91_full_validation.pdf.gz | 418.6 KB | Display | |
Data in XML | 8p91_validation.xml.gz | 6.2 KB | Display | |
Data in CIF | 8p91_validation.cif.gz | 8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p9/8p91 ftp://data.pdbj.org/pub/pdb/validation_reports/p9/8p91 | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homologyF&H Search |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 9690.183 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Chromobacterium haemolyticum (bacteria) Gene: hfq, B0T39_13335, B0T45_12055, CH06BL_33310, DBB33_18715 Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): E. coli / References: UniProt: A0A1W0CX06 |
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#2: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.75 Å3/Da / Density % sol: 29.7 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 8 Details: #23 of JBScreen Nuc-Pro 1 (Jena Bioscience) 15% PEG4000, 50 mM Tris-HCl, pH 7.5, 150 mM KCl, 20 mM MgCl2 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU PhotonJet-R / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU HyPix-6000HE / Detector: PIXEL / Date: Mar 23, 2023 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→21.32 Å / Num. obs: 13426 / % possible obs: 99.9 % / Redundancy: 5.1 % / CC1/2: 0.996 / Rmerge(I) obs: 0.095 / Rpim(I) all: 0.045 / Rrim(I) all: 0.106 / Χ2: 0.96 / Net I/σ(I): 10.7 / Num. measured all: 68788 |
Reflection shell | Resolution: 1.4→1.42 Å / % possible obs: 100 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.73 / Num. measured all: 2424 / Num. unique obs: 663 / CC1/2: 0.478 / Rpim(I) all: 0.442 / Rrim(I) all: 0.856 / Χ2: 0.88 / Net I/σ(I) obs: 1.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.4→21.32 Å / Cross valid method: FREE R-VALUE / σ(F): 38.87 / Phase error: 30.01 / Stereochemistry target values: TWIN_LSQ_F
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 9.16 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→21.32 Å
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Refine LS restraints |
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LS refinement shell |
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