[English] 日本語
Yorodumi- PDB-2gho: Recombinant Thermus aquaticus RNA polymerase for Structural Studies -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 2gho | ||||||
|---|---|---|---|---|---|---|---|
| Title | Recombinant Thermus aquaticus RNA polymerase for Structural Studies | ||||||
Components |
| ||||||
Keywords | TRANSFERASE / Thermus aquaticus RNA polymerase / recombinant multiprotein complex / coexpression | ||||||
| Function / homology | Function and homology informationDNA-directed RNA polymerase complex / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / protein dimerization activity / DNA-templated transcription / magnesium ion binding / DNA binding / zinc ion binding / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() Thermus aquaticus (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 5 Å | ||||||
Authors | Lamour, V. / Darst, S.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006Title: Recombinant Thermus aquaticus RNA Polymerase for Structural Studies. Authors: Kuznedelov, K. / Lamour, V. / Patikoglou, G. / Chlenov, M. / Darst, S.A. / Severinov, K. | ||||||
| History |
| ||||||
| Remark 999 | SEQUENCE THE BETA PRIME CHAIN D IS AN ENGINEERED TAQ RNA POLYMERASE AND REGION 160-451 OF BETA ...SEQUENCE THE BETA PRIME CHAIN D IS AN ENGINEERED TAQ RNA POLYMERASE AND REGION 160-451 OF BETA PRIME HAS BEEN DELETED AND REPLACED BY A SHORT LINKER GG. |
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 2gho.cif.gz | 364.7 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb2gho.ent.gz | 208.8 KB | Display | PDB format |
| PDBx/mmJSON format | 2gho.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2gho_validation.pdf.gz | 426.8 KB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 2gho_full_validation.pdf.gz | 521 KB | Display | |
| Data in XML | 2gho_validation.xml.gz | 52.5 KB | Display | |
| Data in CIF | 2gho_validation.cif.gz | 80.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gh/2gho ftp://data.pdbj.org/pub/pdb/validation_reports/gh/2gho | HTTPS FTP |
-Related structure data
| Similar structure data |
|---|
-
Links
-
Assembly
| Deposited unit | ![]()
| ||||||||
|---|---|---|---|---|---|---|---|---|---|
| 1 |
| ||||||||
| Unit cell |
|
-
Components
| #1: Protein | Mass: 34830.895 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Thermus aquaticus (bacteria) / Gene: rpoA / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: ![]() #2: Protein | | Mass: 124930.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Thermus aquaticus (bacteria) / Gene: rpoB / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: ![]() #3: Protein | | Mass: 138693.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Thermus aquaticus (bacteria) / Gene: rpoC / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: ![]() |
|---|
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
|---|
-
Sample preparation
| Crystal | Density Matthews: 5.04 Å3/Da / Density % sol: 75.6 % |
|---|---|
| Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 0.05 M Na cacodylate 10 mM MgCl2 1.0 M Li2SO4, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
| Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 |
|---|---|
| Detector | Detector: CCD / Date: May 5, 2005 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Relative weight: 1 |
| Reflection | Resolution: 4.1→25 Å / Num. obs: 50317 / Rsym value: 0.081 |
| Reflection shell | Resolution: 4.1→4.25 Å / % possible all: 93.5 |
-
Processing
| Software |
| ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 5→25 Å / σ(F): 0
| ||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 5→25 Å
| ||||||||||||||||||||||||
| Xplor file | Serial no: 1 / Param file: CNS_TOPPAR:protein_rep.param |
Movie
Controller
About Yorodumi




Thermus aquaticus (bacteria)
X-RAY DIFFRACTION
Citation







PDBj



