Search Count: 12
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Human Cytoplasmic Dynein N-Terminus Dimerization Domain At 1.8 Angstrom Resolution
Organism: Homo sapiens
Method: X-RAY DIFFRACTION Resolution:1.79 Å Release Date: 2018-07-11 Classification: MOTOR PROTEIN Ligands: GOL, MG, CA, NA, K |
Organism: Homo sapiens
Method: X-RAY DIFFRACTION
Release Date: 2018-07-11
Ligands: GOL, MG, CA, NA, K
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Cryo-Em Structure Of Two Dynein Tail Domains Bound To Dynactin And Bicdr1
Organism: Mus musculus, Homo sapiens, Sus scrofa
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN Ligands: ADP, ATP |
Organism: Mus musculus, Homo sapiens, Sus scrofa
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
Ligands: ADP, ATP
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N Terminal Region Of Dynein Tail Domains In Complex With Dynactin Filament And Bicdr-1
Organism: Homo sapiens, Mus musculus, Sus scrofa
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN Ligands: ADP |
Organism: Homo sapiens, Mus musculus, Sus scrofa
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
Ligands: ADP
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C Terminal Region Of The Dynein Heavy Chains In The Dynein Tail/Dynactin/Bicdr1 Complex
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN |
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
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Dynein Light Intermediate Chain Region Of The Dynein Tail/Dynactin/Bicdr1 Complex
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN |
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
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Roadblock-1 Region Of The Dynein Tail/Dynactin/Bicdr1 Complex
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN |
Organism: Homo sapiens
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
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Cryo-Em Structure Of Two Dynein Tail Domains Bound To Dynactin And Hook3
Organism: Homo sapiens, Sus scrofa
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN Ligands: ADP, ATP |
Organism: Homo sapiens, Sus scrofa
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
Ligands: ADP, ATP
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Cryo-Em Structure Of A Single Dynein Tail Domain Bound To Dynactin And Bicd2N
Organism: Homo sapiens, Mus musculus, Sus scrofa
Method: ELECTRON MICROSCOPY Release Date: 2018-01-17 Classification: MOTOR PROTEIN Ligands: ADP, ATP |
Organism: Homo sapiens, Mus musculus, Sus scrofa
Method: ELECTRON MICROSCOPY
Release Date: 2018-01-17
Ligands: ADP, ATP
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Escherichia Coli Replication Terminator Protein (Tus) Complexed With Dna- G/T Mismatch.
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION Resolution:2.80 Å Release Date: 2015-08-26 Classification: REPLICATION/DNA Ligands: IOD, MPD |
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION
Release Date: 2015-08-26
Ligands: IOD, MPD
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Escherichia Coli Replication Terminator Protein (Tus) Complexed With Dna- Ag/At Mismatch.
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION Resolution:2.40 Å Release Date: 2015-08-26 Classification: REPLICATION/DNA Ligands: IOD, MPD |
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION
Release Date: 2015-08-26
Ligands: IOD, MPD
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Escherichia Coli Replication Terminator Protein (Tus) H114A Mutant Complexed With Dna- Tera Lock.
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION Resolution:2.35 Å Release Date: 2015-08-26 Classification: REPLICATION/DNA Ligands: IOD, MPD, EDO |
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION
Release Date: 2015-08-26
Ligands: IOD, MPD, EDO
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Escherichia Coli Replication Terminator Protein (Tus) Complexed With Dna- Gc(6) Swapped.
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION Resolution:2.70 Å Release Date: 2015-08-26 Classification: REPLICATION/DNA Ligands: IOD, MPD |
Organism: Escherichia coli (strain k12), Escherichia coli
Method: X-RAY DIFFRACTION
Release Date: 2015-08-26
Ligands: IOD, MPD
