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Open data
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Basic information
Entry | Database: PDB / ID: 1cuk | ||||||
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Title | ESCHERICHIA COLI RUVA PROTEIN AT PH 4.9 AND ROOM TEMPERATURE | ||||||
![]() | RUVA PROTEIN | ||||||
![]() | HELICASE / DNA REPAIR / SOS RESPONSE / DNA-BINDING / DNA RECOMBINATION | ||||||
Function / homology | ![]() Holliday junction helicase complex / Holliday junction resolvase complex / four-way junction helicase activity / recombinational repair / SOS response / four-way junction DNA binding / response to radiation / ATP binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Rafferty, J.B. / Rice, D.W. | ||||||
![]() | ![]() Title: Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Authors: Rafferty, J.B. / Sedelnikova, S.E. / Hargreaves, D. / Artymiuk, P.J. / Baker, P.J. / Sharples, G.J. / Mahdi, A.A. / Lloyd, R.G. / Rice, D.W. #1: ![]() Title: Crystallization of E.Coli Ruva Gives Insights Into the Symmetry of a Holliday Junction/Protein Complex Authors: Sedelnikova, S.E. / Rafferty, J.B. / Hargreaves, D. / Mahdi, A.A. / Lloyd, R.G. / Rice, D.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.1 KB | Display | ![]() |
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PDB format | ![]() | 33.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.4 KB | Display | ![]() |
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Full document | ![]() | 376.3 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 22197.783 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Sedelnikova, S.E., (1999) Acta Crystallogr. D., 55, 263. PH range low: 7.5 / PH range high: 6.5 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Oct 26, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 16391 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rmerge(I) obs: 0.073 |
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Processing
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Refinement | Resolution: 1.9→15 Å / σ(F): 0 Details: THE B-FACTORS FOR THE C-TERMINAL SEGMENT OF THE PROTEIN (RESIDUES 107 - 203) ARE HIGH WITH AN AVERAGE VALUE OF 73.6 A**2 OVER ALL ATOMS (71.0A**2 FOR MAIN CHAIN) AND THUS REPRESENT ...Details: THE B-FACTORS FOR THE C-TERMINAL SEGMENT OF THE PROTEIN (RESIDUES 107 - 203) ARE HIGH WITH AN AVERAGE VALUE OF 73.6 A**2 OVER ALL ATOMS (71.0A**2 FOR MAIN CHAIN) AND THUS REPRESENT POSITIONAL UNCERTAINTY OF APPROXIMATELY 1A IN SOME REGIONS.
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Refinement step | Cycle: LAST / Resolution: 1.9→15 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.209 / Rfactor Rfree: 0.027 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_plane_restr / Dev ideal: 0.008 / Weight: 5 |