+Open data
-Basic information
Entry | Database: PDB / ID: 6uhq | |||||||||
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Title | Crystal Structure of C148 mGFP-cDNA-3 | |||||||||
Components | C148 mGFP-cDNA-3 | |||||||||
Keywords | FLUORESCENT PROTEIN / green fluorescent protein / beta-barrel / DNA / protein-DNA conjugate | |||||||||
Function / homology | Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / bioluminescence / generation of precursor metabolites and energy / Unknown ligand / Green fluorescent protein Function and homology information | |||||||||
Biological species | Aequorea victoria (jellyfish) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å | |||||||||
Authors | Winegar, P.W. / Hayes, O.G. / McMillan, J.R. / Figg, C.A. / Focia, P.J. / Mirkin, C.A. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Chem / Year: 2020 Title: DNA-Directed Protein Packing within Single Crystals. Authors: Winegar, P.H. / Hayes, O.G. / McMillan, J.R. / Figg, C.A. / Focia, P.J. / Mirkin, C.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6uhq.cif.gz | 62 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6uhq.ent.gz | 41.1 KB | Display | PDB format |
PDBx/mmJSON format | 6uhq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uh/6uhq ftp://data.pdbj.org/pub/pdb/validation_reports/uh/6uhq | HTTPS FTP |
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-Related structure data
Related structure data | 6uhjC 6uhkC 6uhlC 6uhmC 6uhnC 6uhoC 6uhpC 6uhrC 5n9oS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 31038.908 Da / Num. of mol.: 1 / Mutation: S148C Source method: isolated from a genetically manipulated source Details: This mutant of EGFP has a single surface cysteine at residue 148 (counting from M37 and counting CRO as 3 residues) and an N-terminal his-tag. Source: (gene. exp.) Aequorea victoria (jellyfish) / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P42212*PLUS |
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#2: Chemical | ChemComp-UNL / Mass: 32.065 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: 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: 2.31 Å3/Da / Density % sol: 46.74 % / Description: Green crystals |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 1 microliter C148 mGFP-cDNA-3 (5 mg/mL (protein concentration) in 10 mM Tris Buffer pH 7.4, 137 mM NaCl) + 1 microliter crystallization condition (0.1 M MES pH 6.5, 30% (w/v) PEG 4000) in a ...Details: 1 microliter C148 mGFP-cDNA-3 (5 mg/mL (protein concentration) in 10 mM Tris Buffer pH 7.4, 137 mM NaCl) + 1 microliter crystallization condition (0.1 M MES pH 6.5, 30% (w/v) PEG 4000) in a sitting drop with a 70 microliter reservoir (0.1 M MES pH 6.5, 30% (w/v) PEG 4000) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Dec 1, 2018 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.85→53.159 Å / Num. all: 6723 / Num. obs: 6723 / % possible obs: 99.3 % / Redundancy: 3.3 % / Rpim(I) all: 0.112 / Rrim(I) all: 0.212 / Rsym value: 0.178 / Net I/av σ(I): 3.8 / Net I/σ(I): 5.8 / Num. measured all: 21886 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5N9O Resolution: 2.85→50.04 Å / Cor.coef. Fo:Fc: 0.936 / Cor.coef. Fo:Fc free: 0.838 / WRfactor Rfree: 0.2572 / WRfactor Rwork: 0.169 / FOM work R set: 0.7896 / SU B: 17.317 / SU ML: 0.331 / SU R Cruickshank DPI: 0.8051 / SU Rfree: 0.4339 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.805 / ESU R Free: 0.434 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 98.2 Å2 / Biso mean: 29.422 Å2 / Biso min: 1.18 Å2
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Refinement step | Cycle: final / Resolution: 2.85→50.04 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.85→2.924 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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