Cryo-em structure

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Unknown (4383)
Proteomics (257)
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Organisms

Aerococcus urinae NBRC 15544 = CCUG 36881 (208)
Allexis (208)
Apostichopus japonicus (208)
Canis lupus familiaris (208)
Carya cathayensis (208)
Clostridioides difficile 630 (208)
Cyanophora paradoxa (208)
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synthetic construct (2)
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Escherichia coli BW25113 (1)
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synthetic construct (1)
Escherichia coli str. K-12 substr. MG1655 (1)
Drosophila melanogaster (1)
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Repository

pride (208)
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geo (65)
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Transthyretin amyloidosis (1)

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Mass Spectrometry (208)
Chemical cross-linking coupled with mass spectrometry proteomics (68)
Shotgun proteomics (45)
Bottom-up proteomics (42)
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HDMSE (15)
Affinity purification coupled with mass spectrometry proteomics (13)
Gel-based experiment (13)
MSE (12)
Data-independent acquisition (7)
Top-down proteomics (3)
Mass spectrometry (2)
Glycoproteomics (2)
SRM/MRM (2)
SWATH MS (2)
Mass spectrometry assay (1)
All-ion fragmentation (1)
DiaPASEF (1)

Instrument Platform

Orbitrap Fusion Lumos (6)
Q Exactive (3)
LTQ Orbitrap (2)
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LTQ (1)
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Orbitrap Exploris 480 (1)
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Q Exactive HF (1)
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Q Exactive UHMR (1)
TimsTOF Pro 2 (1)
Direct infusion MS - positive - - Ditect Injection MS (1)
Liquid Chromatography MS (Negative) (1)
Liquid Chromatography MS (Positive) (1)
MS Imaging - positive - - Cryogenic OrbiSIMS TOF Image (1)
MS Imaging - negative - - Cryogenic OrbiSIMS Image (1)
MS Imaging - positive - - Cryogenic OrbiSIMS (1)
MS Imaging - negative - - Cryogenic OrbiSIMS (Negative) (1)
MS Imaging - positive - - Cryogenic OrbiSIMS (Positive) (1)
MS Imaging - positive - - Cryogenic ToF-SIMS (1)
Gas Chromatography MS (1)
Liquid Chromatography MS - negative - reverse phase (1)

Publication Date

2025 (63)
2024 (59)
2026 (53)
2023 (40)
2022 (39)
2021 (26)
2019 (17)
2020 (13)
2018 (6)
2017 (5)
2016 (2)
2015 (1)
2012 (1)

CHEBI ID

CHEBI:194455 (1)
CHEBI:194482 (1)
CHEBI:30512 (1)
CHEBI:29287 (1)
CHEBI:24835 (1)
CHEBI:48591 (1)
CHEBI:39270 (1)
CHEBI:24059 (1)
CHEBI:50917 (1)
CHEBI:24402 (1)
CHEBI:32955 (1)
CHEBI:36735 (1)
CHEBI:38776 (1)
CHEBI:59659 (1)
CHEBI:38193 (1)
CHEBI:25340 (1)
CHEBI:33833 (1)
CHEBI:48835 (1)
CHEBI:77383 (1)
CHEBI:38670 (1)
CHEBI:37739 (1)
CHEBI:38314 (1)
CHEBI:38093 (1)
CHEBI:24955; CHEBI:52898 (1)
CHEBI:38976; CHEBI:36820 (1)
CHEBI:38669 (1)
CHEBI:48588 (1)
CHEBI:47985 (1)
CHEBI:23245 (1)
CHEBI:39307 (1)

Metabolite Name

Cerium(3+) trihydride (1)
3-(4-hydroxyphenyl)-1-[2,4,6-trihydroxy-3,5-bis(3-methylbut-2-en-1-yl)phenyl]propan-1-one (1)
N-Acetyl-L-valyl-L-valyl-L-valyl-L-valyl-L-valyl-N-methyl-L-valinamide (1)
N-[(3,5-ditert-butyl-4-hydroxyphenyl)methyl]-2-dimethoxyphosphorylacetamide (1)
?D-?Xylonic acid (1)
3,4,5-trihydroxy-6-({5-hydroxy-11-methoxy-16,18-dioxo-6,8,19-trioxapentacyclo[10.7.0.0?,?.0?,?.0??,??]nonadeca-1(12),2(9),10,13(17)-tetraen-4-yl}oxy)oxane-2-carboxylic acid (1)
PG(20:0/22:4(7Z,10Z,13Z,16Z)) (1)
Benzene, 1,1',1'',1''',1'''',1'''''-(bi-2-cyclopropen-1-yl)-1,1',2,2',3,3'-hexaylhexakis- (1)
PtdIns-(3,4,5)-P3 (1,2-dioctanoyl) (1)
PI(13:0/18:3(6Z,9Z,12Z)) (1)
FD&C Green No. 1 (1)
(2E)-3-phenyl-1-[2,4,6-trihydroxy-3-(4-hydroxy-3-methylbut-2-en-1-yl)-5-(3-methylbut-2-en-1-yl)phenyl]prop-2-en-1-one (1)
1,2,3-Tris(decyloxy)-5-isocyanatobenzene (1)
Lauryl hydroxysultaine (1)
L-Tyrosyl-L-seryl-L-threonyl-L-isoleucyl-L-histidyl-L-prolyl-L-alanyl-L-serine (1)
N-[6-[bis-(4-methylphenyl)sulfonylamino]hexyl]-4-methyl-N-(4-methylphenyl)sulfonylbenzenesulfonamide (1)
Decanoic acid, monoamide with N-(2-aminoethyl)-1,2-ethanediamine (1)
2,5-Bis(8-butoxy-2,6-dimethyloctan-2-yl)benzene-1,4-diol (1)
Germane, acetoxytrimethyl- (1)
L-Prolyl-L-prolyl-L-alanyl-L-alanyl-L-alanylglycylglycyl-L-methionine (1)
AC1NQZVR (1)
Peptide 7194 (1)
L-Lysyl-N~5~-(diaminomethylidene)-L-ornithyl-L-glutaminyl-L-lysyl-L-threonine (1)
4-(3,7-dimethylocta-2,6-dien-1-yl)-5-(6-hydroxy-1-benzofuran-2-yl)benzene-1,3-diol (1)
PG(P-16:0/12:0) (1)
2,6-Dicyclohexyl-1,4-diethyl-1,4-dihydropyridine-3,5-dicarboxylate (1)
L-Serine, L-arginyl-L-leucyl-L-valyl-L-leucylglycyl- (1)
(2S,2'S)-2,2'-[Propane-1,3-diylbis(dodecanoylazanediyl)]dipropanoic acid (non-preferred name) (1)
Beta-Alanine, N-(7-oxo-1,3,5-cycloheptatrien-1-yl)-, 2-(diethylamino)ethyl ester, citrate (1:1) (1)
Piperidine, 1-((4-methyl-1-piperazinyl)acetyl)-2,2,6,6-tetramethyl- (1)

First Public Date

2025 (25)
2024 (23)
2026 (16)
2023 (7)
2022 (6)
2021 (5)
2020 (4)
2019 (2)
2017 (2)
2018 (1)
2015 (1)

Classification

bacteria (5)
viruses (2)

Study type

Other (1)
Transcription profiling by array (1)

Release Date

2025 (611)
2024 (606)
2023 (570)
2022 (567)
2021 (477)
2020 (392)
2019 (264)
2018 (209)
2026 (148)
2017 (147)
2016 (113)
2015 (59)
2012 (48)
2014 (39)
2013 (35)
2011 (22)
2008 (17)
2009 (16)
2010 (13)
2007 (10)
2006 (7)
2005 (5)
2003 (3)
2002 (3)
2004 (2)
2001 (1)
1998 (1)

Lab affiliation

Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University, Shanghai, China (5)
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA., Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA (3)
NovAliX, Department of Biophysics, 16 Rue d’Ankara, 67000, Strasbourg, France; orcid.org/0000-0001-6229-4524 (3)
UCSF (3)
1 Interdisciplinary Research Center on Biology and Chemistry, State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China 2 Shanghai Academy of Natural Sciences (SANS), Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China (2)
Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia (2)
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute of Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands (2)
Department of Biochemistry and Molecular Biology School of Medicine, Oregon Health & Science University 3181 SW Sam Jackson Park Road Portland, OR 97239, USA (2)
Department of Biochemistry, The University of British Columbia, Vancouver, Canada (2)
Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas 75390, USA (2)
Functional Proteomics, ICR (2)
King's College London, Chemistry Department, 7 Trinity Street, London, SE1 1DB, UK (2)
Kobilka Institute of Innovative Drug Discovery, School of Medicine, The Chinese University of Hong Kong, Shenzhen, Shenzhen 518172, China. (2)
Kobilka Institute of Innovative Drug Discovery, School ofMedicine, The Chinese University of Hong Kong, Shenzhen, China, 518172 (2)
Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, Villigen, Switzerland; Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zurich, Switzerland (2)
Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark (2)
University of Pennsylvania (2)
Westlake University (2)
1 Interdisciplinary Research Center on Biology and Chemistry, State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China 2 Shanghai Academy of Natural Sciences (SANS), Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 201210, China (lab head) (1)
1. Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada; 2. University of Victoria Genome BC Proteomics Centre, University of Victoria, Victoria, British Columbia, Canada; 3. Gerald Bronfman Department of Oncology, Jewish General Hospital, Montreal, Quebec, Canada; 4. Segal Cancer Proteomics Centre, Lady Davis Institute, Jewish General Hospital, McGill University, Montreal, Quebec, Canada (1)
1. Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, 3052, Victoria, Australia and Department of Medical Biology, The University of Melbourne, Royal Parade, Parkville, 3052, Victoria, Australia (1)
Associate Professor, Department of Chemistry Associate Professor, Thomas C. Jenkins Department of Biophysics Associate Professor, Department of Biology (1)
Bioanalytical Mass Spectrometry Group Max Planck Institute for Multidisciplinary Sciences Germany Bioanalytics Institute for Clinical Chemistry University Medical Center Goettingen Germany (1)
Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany University Medical Center Göttingen, Institute of Clinical Chemistry, Bioanalytics Group, Göttingen, Germany Cluster of Excellence "Multiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells" (MBExC), University of Göttingen, Germany (1)
Bioanalytical Mass spectroscopy Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Germany (1)
Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3BF, Scotland, United Kingdom (1)
Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany. Wellcome Center for Cell Biology, University of Edinburgh, Edinburgh, EH9 3BF, United Kingdom. (1)
Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany (1)
Biochemistry and Molecular Biology, Indiana University School of Medicine (1)
Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, USA (1)

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Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

PRJNA623561 | ENA

Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

Setd2 methylate the nucleosome to form H3K36me3. Here we utilized the Cryo-EM to elucidate the structure of SETD2/Set2 bound with nucleosomes. Through this structure analysis, we found that histone H1 may interfere the enzymatic activity of SETD2/Set2 by inhibiting their binding affinity.

ORGANISM(S): Homo sapiens

2021-05-20 | GSE148235 | GEO

Cryo-EM structure of human hexameric MCM2-7 complex.

Not available

S-EPMC9475327 | biostudies-literature

Cryo-EM structure of the human histamine H₁ receptor/G_q complex.

Not available

S-EPMC8027608 | biostudies-literature

Cryo-EM structure of the extracellular domain of murine Thrombopoietin Receptor in complex with Thrombopoietin.

The haematopoietic cytokine thrombopoietin (Tpo) is the primary regulator of megakaryocyte and platelet numbers and is required for maintenance of the haematopoetic stem cell compartment. Tpo is a heavily glycosylated, hepatocyte-derived cytokine which functions by binding to its receptor (TpoR) on ...

ORGANISM(S): Homo sapiens (Human)

2024-01-09 | PXD046926 | Pride

Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1

PRJNA1428774 | ENA

In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM.

Not available

S-EPMC9388967 | biostudies-literature

Cryo-EM structure of haemoglobin at 3.2 A determined with the Volta phase plate.

Not available

S-EPMC5497076 | biostudies-literature

Cryo-EM structures of the human Elongator complex at work

The deposited data concern the mapping of acetylation sites on wild-type and the K280A, Y363A mutants of Elp3 by LC-MS/MS. Abstract of the manuscript: tRNA modifications affect ribosomal elongation speed and co-translational folding dynamics. The Elongator complex is responsible for introducing 5-ca...

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

MSV000092998 | MassIVE

Cryo-EM of dynamic protein complexes in eukaryotic DNA replication.

Not available

S-EPMC5192969 | biostudies-literature

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