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Showing all 49 items for (author: kawahara & r)

EMDB-63297:
Cryo-EM map of collagenase H (E416Q mutant) from Hathewaya histolytica bound to C-terminal region of collagen model peptide (Pro-Hyp-Gly)10
Method: single particle / : Oki H, Kawahara K

EMDB-63331:
Consensus map of apo collagenase H from Hathewaya histolytica
Method: single particle / : Oki H, Kawahara K

EMDB-63332:
Cryo-EM map of apo collagenase H from Hathewaya histolytica - focused map of the Peptidase-Helper-PKD1 domains
Method: single particle / : Oki H, Kawahara K

EMDB-63333:
Cryo-EM map of apo collagenase H from Hathewaya histolytica - focused map of the ARM domain
Method: single particle / : Oki H, Kawahara K

EMDB-63334:
Consensus map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)10
Method: single particle / : Oki H, Kawahara K

EMDB-63335:
Cryo-EM map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)10 - focused map of ColH bound to the C-terminal region of collagen model peptide
Method: single particle / : Oki H, Kawahara K

EMDB-63336:
Cryo-EM map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)10 - focused map of ColH bound to the N-terminal region of collagen model peptide
Method: single particle / : Oki H, Kawahara K

EMDB-63337:
Composite map of apo collagenase H from Hathewaya histolytica
Method: single particle / : Oki H, Kawahara K

EMDB-63339:
Composite map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)10
Method: single particle / : Oki H, Kawahara K

EMDB-63508:
Consensus map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12
Method: single particle / : Oki H, Kawahara K

EMDB-63509:
Cryo-EM map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12 - focused map of the ARM domain
Method: single particle / : Oki H, Kawahara K

EMDB-63510:
Cryo-EM map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12 - focused map of the Peptidase-Helper-PKD1 domains
Method: single particle / : Oki H, Kawahara K

EMDB-63511:
Composite map of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12
Method: single particle / : Oki H, Kawahara K

EMDB-65889:
Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica bound to C-terminal region of the collagen-binding protein ColH (Pro-Pro-Gly)10
Method: single particle / : Oki H, Kawahara K

PDB-9lqj:
Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica bound to C-terminal region of collagen model peptide (Pro-Hyp-Gly)10
Method: single particle / : Oki H, Kawahara K

PDB-9lrk:
Cryo-EM structure of apo collagenase H from Hathewaya histolytica
Method: single particle / : Oki H, Kawahara K

PDB-9lrm:
Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)10
Method: single particle / : Oki H, Kawahara K

PDB-9lyi:
Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12
Method: single particle / : Oki H, Kawahara K

PDB-9wdc:
Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica bound to C-terminal region of the collagen-binding protein ColH (Pro-Pro-Gly)10
Method: single particle / : Oki H, Kawahara K

EMDB-60902:
Cryo-EM structure of the type IVb pilus from enterotoxigenic Escherichia coli
Method: helical / : Kawahara K, Oki H, Nakamura S

EMDB-60903:
Cryo-EM structure of the type I pilus from enterotoxigenic Escherichia coli
Method: helical / : Kawahara K, Oki H, Nakamura S

PDB-9iuf:
Cryo-EM structure of the type IVb pilus from enterotoxigenic Escherichia coli
Method: helical / : Kawahara K, Oki H, Nakamura S

PDB-9iug:
Cryo-EM structure of the type I pilus from enterotoxigenic Escherichia coli
Method: helical / : Kawahara K, Oki H, Nakamura S

EMDB-62272:
Consensus map of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3
Method: single particle / : Shihoya W, Akasaka H, Nureki O

EMDB-62273:
focused on refinement endothelin receptor type-B of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3
Method: single particle / : Akasaka H, Shihoya W, Nureki O

EMDB-62274:
CryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3
Method: single particle / : Shihoya W, Akasaka H, Nureki O

EMDB-62275:
CryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in the ligand-free form
Method: single particle / : Shihoya W, Akasaka H, Nureki O

PDB-9kdf:
CryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in complex with RES-701-3
Method: single particle / : Shihoya W, Akasaka H, Nureki O

PDB-9kdg:
CryoEM structure of Calcineurin-fusion Human endothelin receptor type-B in the ligand-free form
Method: single particle / : Shihoya W, Akasaka H, Nureki O

EMDB-38215:
Human GPR34 -Gi complex bound to S3E-LysoPS
Method: single particle / : Kawahara R, Shihoya W, Nureki O

EMDB-38217:
Human GPR34 -Gi complex bound to S3E-LysoPS, receptor focused
Method: single particle / : Kawahara R, Shihoya W, Nureki O

PDB-8xbe:
Human GPR34 -Gi complex bound to S3E-LysoPS
Method: single particle / : Kawahara R, Shihoya W, Nureki O

PDB-8xbg:
Human GPR34 -Gi complex bound to S3E-LysoPS, receptor focused
Method: single particle / : Kawahara R, Shihoya W, Nureki O

EMDB-38218:
Human GPR34 -Gi complex bound to M1
Method: single particle / : Kawahara R, Shihoya W, Nureki O

EMDB-38219:
Human GPR34 -Gi complex bound to M1, receptor focused
Method: single particle / : Kawahara R, Shihoya W, Nureki O

PDB-8xbh:
Human GPR34 -Gi complex bound to M1
Method: single particle / : Kawahara R, Shihoya W, Nureki O

PDB-8xbi:
Human GPR34 -Gi complex bound to M1, receptor focused
Method: single particle / : Kawahara R, Shihoya W, Nureki O

EMDB-33643:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab816
Method: single particle / : Uchikubo T, Shirouzu M

EMDB-33644:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab803
Method: single particle / : Uchikubo T, Shirouzu M

PDB-7y6l:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab816
Method: single particle / : Uchikubo T, Shirouzu M

PDB-7y6n:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab803
Method: single particle / : Uchikubo T, Shirouzu M

EMDB-33065:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab765
Method: single particle / : Kamada K, Shirouzu M

EMDB-33066:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab712
Method: single particle / : Kamada K, Shirouzu M

EMDB-33067:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab709
Method: single particle / : Kamada K, Shirouzu M

EMDB-33068:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab847
Method: single particle / : Kamada K, Shirouzu M

PDB-7x93:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab765
Method: single particle / : Kamada K, Shirouzu M

PDB-7x94:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab712
Method: single particle / : Kamada K, Shirouzu M

PDB-7x95:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab709
Method: single particle / : Kamada K, Shirouzu M

PDB-7x96:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab847
Method: single particle / : Kamada K, Shirouzu M

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New format data for meta-information of EMDB entries

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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

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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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