Search Count: 12
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor1 At Ph 4.3 In Detergent
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY Resolution:2.94 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LFA, RET |
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LFA, RET
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor1 At Ph 8.0 In Nanodisc
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY Resolution:2.43 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LFA, RET |
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LFA, RET
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor1 At Ph 8.0 In Detergent
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY Resolution:2.87 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LMT, LFA, RET |
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LMT, LFA, RET
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor1 At Ph 10.5 In Detergent In The Ground State
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY Resolution:2.70 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LMT, RET, LFA |
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LMT, RET, LFA
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor1 At Ph 10.5 In Detergent In The M State
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY Resolution:2.30 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LMT, RET |
Organism: Cryobacterium levicorallinum
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LMT, RET
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Cryo-Em Structure Of The Microbial Rhodopsin Cryor2 At Ph 8.0 In Detergent
Organism: Subtercola endophyticus
Method: ELECTRON MICROSCOPY Resolution:2.44 Å Release Date: 2025-05-14 Classification: MEMBRANE PROTEIN Ligands: LFA, RET |
Organism: Subtercola endophyticus
Method: ELECTRON MICROSCOPY
Release Date: 2025-05-14
Ligands: LFA, RET
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Crystal Structure Of The Viral Rhodopsins Chimera O1O2
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION Resolution:1.96 Å Release Date: 2020-11-25 Classification: MEMBRANE PROTEIN Ligands: LFA, RET |
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION
Release Date: 2020-11-25
Ligands: LFA, RET
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Crystal Structure Of The Viral Rhodopsin Olpvr1 In P1 Space Group
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION Resolution:1.60 Å Release Date: 2020-11-25 Classification: MEMBRANE PROTEIN Ligands: LFA, OLA, OLC |
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION
Release Date: 2020-11-25
Ligands: LFA, OLA, OLC
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Crystal Structure Of The Viral Rhodopsin Olpvr1 In P21212 Space Group
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION Resolution:1.40 Å Release Date: 2020-11-25 Classification: MEMBRANE PROTEIN Ligands: LFA, 97N |
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION
Release Date: 2020-11-25
Ligands: LFA, 97N
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Crystal Structure Of Viral Rhodopsin Olpvrii
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION Resolution:1.90 Å Release Date: 2019-11-06 Classification: MEMBRANE PROTEIN Ligands: LFA, RET, OLB |
Organism: Organic lake phycodnavirus
Method: X-RAY DIFFRACTION
Release Date: 2019-11-06
Ligands: LFA, RET, OLB
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Electron Cryo-Microscopy Structure Of The Canonical Trpc4 Ion Channel
Organism: Danio rerio
Method: ELECTRON MICROSCOPY Release Date: 2018-05-02 Classification: TRANSPORT PROTEIN Ligands: Y01, 44E |
Organism: Danio rerio
Method: ELECTRON MICROSCOPY
Release Date: 2018-05-02
Ligands: Y01, 44E
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Crystal Structure Of The Inward H(+) Pump Xenorhodopsin
Organism: Nanosalina sp. (strain j07ab43)
Method: X-RAY DIFFRACTION Resolution:2.50 Å Release Date: 2017-12-13 Classification: MEMBRANE PROTEIN Ligands: RET, LFA, MUN |
Organism: Nanosalina sp. (strain j07ab43)
Method: X-RAY DIFFRACTION
Release Date: 2017-12-13
Ligands: RET, LFA, MUN