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Showing all 18 items for (author: gerlach & p)

EMDB-14510:
Human NEXT dimer - overall reconstruction of the core complex
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

EMDB-14511:
Human NEXT dimer - focused reconstruction of the dimerization module
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

EMDB-14513:
Human NEXT dimer - focused reconstruction of the single MTR4
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

EMDB-14514:
Human NEXT dimer - single protomer
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

EMDB-14515:
Human NEXT dimer in complex with the nuclear RNA exosome
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

PDB-7z4y:
Human NEXT dimer - overall reconstruction of the core complex
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

PDB-7z4z:
Human NEXT dimer - focused reconstruction of the dimerization module
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

PDB-7z52:
Human NEXT dimer - focused reconstruction of the single MTR4
Method: single particle / : Gerlach P, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Conti E

EMDB-11093:
Cryo-EM map of La Crosse virus polymerase at pre-initiation stage
Method: single particle / : Arragain B, Effantin G

EMDB-11095:
Masked cryo-EM map of La Crosse virus polymerase cap-binding domain and mid domain
Method: single particle / : Arragain B, Effantin G, Schoehn G, Cusack S, Malet H

EMDB-11107:
Masked cryo-EM map of La Crosse virus polymerase zinc-binding domain and mid domain
Method: single particle / : Arragain B, Effantin G, Schoehn G, Cusack S, Malet H

EMDB-11118:
La Crosse virus polymerase at elongation mimicking stage
Method: single particle / : Arragain B, Effantin G

PDB-6z6g:
Cryo-EM structure of La Crosse virus polymerase at pre-initiation stage
Method: single particle / : Arragain B, Effantin G, Gerlach P, Reguera J, Schoehn G, Cusack S, Malet H

PDB-6z8k:
La Crosse virus polymerase at elongation mimicking stage
Method: single particle / : Arragain B, Effantin G, Schoehn G, Cusack S, Malet H

EMDB-0128:
Human nuclear RNA exosome EXO-10-MPP6 complex
Method: single particle / : Gerlach P, Schuller JM, Falk S, Basquin J, Conti E

PDB-6h25:
Human nuclear RNA exosome EXO-10-MPP6 complex
Method: single particle / : Gerlach P, Schuller JM, Falk S, Basquin J, Conti E

EMDB-0127:
Human nuclear RNA exosome EXO-14 complex
Method: single particle / : Gerlach P, Schuller JM, Falk S, Basquin J, Conti E

EMDB-2930:
Cryo-electron microscopy map of La Crosse orthobunyavirus polymerase (apo form, residues 1-1750)
Method: single particle / : Gerlach P, Malet H, Cusack S, Reguera J

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Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

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Oct 5, 2021. Nobel Prize for mechanically activated and temperature-gated ion channels

Nobel Prize for mechanically activated and temperature-gated ion channels

  • The Nobel Prize in Physiology or Medicine 2021 was awarded jointly to David Julius and Ardem Patapoutian "for their discoveries of receptors for temperature and touch."
  • EM Navigator can help to find cryo-EM structure data by both pioneers.

External links:The Nobel Prize in Physiology or Medicine 2021 - NobelPrize.org / Structure data by Ardem Patapoutian / Structure data by David Julius

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Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

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Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

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