+Open data
-Basic information
Entry | Database: PDB / ID: 1grj | ||||||
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Title | GREA TRANSCRIPT CLEAVAGE FACTOR FROM ESCHERICHIA COLI | ||||||
Components | GREA PROTEIN | ||||||
Keywords | TRANSCRIPTION REGULATION / TRANSCRIPT ELONGATION FACTOR / TRANSCRIPT CLEAVAGE FACTOR | ||||||
Function / homology | Function and homology information bacterial-type RNA polymerase holo enzyme binding / DNA-templated transcription elongation / RNA polymerase binding / regulation of DNA-templated transcription elongation / DNA binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.2 Å | ||||||
Authors | Darst, S.A. / Stebbins, C.E. | ||||||
Citation | Journal: Nature / Year: 1995 Title: Crystal structure of the GreA transcript cleavage factor from Escherichia coli. Authors: Stebbins, C.E. / Borukhov, S. / Orlova, M. / Polyakov, A. / Goldfarb, A. / Darst, S.A. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystallization of Grea, a Transcript Cleavage Factor from Escherichia Coli Authors: Darst, S.A. / Stebbins, C.E. / Borukhov, S. / Orlova, M. / Feng, G. / Landick, R. / Goldfarb, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1grj.cif.gz | 50.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1grj.ent.gz | 38 KB | Display | PDB format |
PDBx/mmJSON format | 1grj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1grj_validation.pdf.gz | 364.8 KB | Display | wwPDB validaton report |
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Full document | 1grj_full_validation.pdf.gz | 372.3 KB | Display | |
Data in XML | 1grj_validation.xml.gz | 5.5 KB | Display | |
Data in CIF | 1grj_validation.cif.gz | 8.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gr/1grj ftp://data.pdbj.org/pub/pdb/validation_reports/gr/1grj | HTTPS FTP |
-Related structure data
Similar structure data |
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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: 17662.928 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cell line: XL1-BLUE / References: UniProt: P0A6W5 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.11 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 1.5418 |
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Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Jan 4, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40 Å / Num. obs: 8079 / Observed criterion σ(I): 1 / Redundancy: 15.1 % / Rmerge(I) obs: 0.054 |
Reflection | *PLUS % possible obs: 85.5 % / Redundancy: 3.8 % / Num. measured all: 30813 / Rmerge(I) obs: 0.072 |
-Processing
Software |
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Refinement | Resolution: 2.2→6 Å / σ(F): 1
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Displacement parameters | Biso mean: 24.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |