Dr. Virgile Adam, PhD - CNRS / Institute for Structural Biology (IBS) - Research scientist

Dr. Virgile Adam

PhD

CNRS / Institute for Structural Biology (IBS)

Research scientist

Grenoble | France

Additional Specialties: single molecule fluorescence microscopy, fluorescent protein engineering, X-ray crystallography

ORCID logohttps://orcid.org/0000-0003-2209-7846

Dr. Virgile Adam, PhD - CNRS / Institute for Structural Biology (IBS) - Research scientist

Dr. Virgile Adam

PhD

Introduction

Primary Affiliation: CNRS / Institute for Structural Biology (IBS) - Grenoble , France

Additional Specialties:

Publications

32Publications

761Reads

2Profile Views

300PubMed Central Citations

Mechanistic investigation of mEos4b reveals a strategy to reduce track interruptions in sptPALM.

Nat Methods 2019 08 8;16(8):707-710. Epub 2019 Jul 8.

University Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.

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http://dx.doi.org/10.1038/s41592-019-0462-3DOI Listing
August 2019
1 Read
32.072 Impact Factor

Arginine 66 Controls Dark-State Formation in Green-to-Red Photoconvertible Fluorescent Proteins.

J Am Chem Soc 2016 Jan 6;138(2):558-65. Epub 2016 Jan 6.

Institut de Biologie Structurale, Université Grenoble Alpes , CEA, CNRS, 38044 Grenoble, France.

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http://dx.doi.org/10.1021/jacs.5b09923DOI Listing
January 2016
23 Reads
5 Citations
12.113 Impact Factor

In cellulo evaluation of phototransformation quantum yields in fluorescent proteins used as markers for single-molecule localization microscopy.

PLoS One 2014 10;9(6):e98362. Epub 2014 Jun 10.

Université Grenoble Alpes, Institut de Biologie Structurale (IBS), Grenoble, France; CNRS, IBS, Grenoble, France; CEA, DSV, IBS, Grenoble, France.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0098362PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4051587PMC
October 2015
33 Reads
5 Citations
3.234 Impact Factor

Remodeling of the Z-Ring Nanostructure during the Streptococcus pneumoniae Cell Cycle Revealed by Photoactivated Localization Microscopy.

MBio 2015 Aug 18;6(4). Epub 2015 Aug 18.

University of Grenoble Alpes, IBS, Grenoble, Franc; CNRS, IBS, Grenoble, France; CEA, IBS, Grenoble, France

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http://dx.doi.org/10.1128/mBio.01108-15DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542196PMC
August 2015
65 Reads
20 Citations
6.790 Impact Factor

Structural basis of photoswitching in fluorescent proteins.

Methods Mol Biol 2014 ;1148:177-202

Institut de Biologie Structurale, Université Grenoble Alpes, Grenoble, France.

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http://dx.doi.org/10.1007/978-1-4939-0470-9_12DOI Listing
December 2014
24 Reads
3 Citations

Phototransformable fluorescent proteins: which one for which application?

Authors:
Virgile Adam

Histochem Cell Biol 2014 Jul 13;142(1):19-41. Epub 2014 Feb 13.

Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, F-38000, Grenoble, France,

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http://dx.doi.org/10.1007/s00418-014-1190-5DOI Listing
July 2014
140 Reads
5 Citations
3.054 Impact Factor

Phototransformable fluorescent proteins: Future challenges.

Curr Opin Chem Biol 2014 Jun 25;20:92-102. Epub 2014 Jun 25.

Univ. Grenoble Alpes, IBS, F-38044 Grenoble, France; CNRS, IBS, F-38044 Grenoble, France; CEA, IBS, F-38044 Grenoble, France. Electronic address:

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http://dx.doi.org/10.1016/j.cbpa.2014.05.016DOI Listing
June 2014
8 Reads
16 Citations
6.813 Impact Factor

Excited state dynamics of the photoconvertible fluorescent protein Kaede revealed by ultrafast spectroscopy.

Photochem Photobiol Sci 2014 Jun;13(6):867-74

Laboratory of Photochemistry and Spectroscopy, Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Heverlee, Belgium.

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http://dx.doi.org/10.1039/c3pp50335fDOI Listing
June 2014
28 Reads
1 Citation
2.270 Impact Factor

In cellulo evaluation of phototransformation quantum yields in fluorescent proteins used as markers for single-molecule localization microscopy.

PLoS ONE 9(6): e98362

PLoS ONE

Single-molecule localization microscopy of biological samples requires a precise knowledge of the employed fluorescent labels. Photoactivation, photoblinking and photobleaching of phototransformable fluorescent proteins influence the data acquisition and data processing strategies to be used in (Fluorescence) Photoactivation Localization Microscopy ((F)-PALM), notably for reliable molecular counting. As these parameters might depend on the local environment, they should be measured in cellulo in biologically relevant experimental conditions. Here, we measured phototransformation quantum yields for Dendra2 fused to actin in fixed mammalian cells in typical (F)-PALM experiments. To this aim, we developed a data processing strategy based on the clustering optimization procedure proposed by Lee et al (PNAS 109, 17436–17441, 2012). Using simulations, we estimated the range of experimental parameters (molecular density, molecular orientation, background level, laser power, frametime) adequate for an accurate determination of the phototransformation yields. Under illumination at 561 nm in PBS buffer at pH 7.4, the photobleaching yield of Dendra2 fused to actin was measured to be (2.5±0.4)×10−5, whereas the blinking-off yield and thermally-activated blinking-on rate were measured to be (2.3±0.2)×10−5 and 11.7±0.5 s−1, respectively. These phototransformation yields differed from those measured in poly-vinyl alcohol (PVA) and were strongly affected by addition of the antifading agent 1,4-diazabicyclo[2.2.2]octane (DABCO). In the presence of DABCO, the photobleaching yield was reduced 2-fold, the blinking-off yield was decreased more than 3-fold, and the blinking-on rate was increased 2-fold. Therefore, DABCO largely improved Dendra2 photostability in fixed mammalian cells. These findings are consistent with redox-based bleaching and blinking mechanisms under (F)-PALM experimental conditions. Finally, the green-to-red photoconversion quantum yield of Dendra2 was estimated to be (1.4±0.6)×10−5 in cellulo under 405 nm illumination.

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June 2014
14 Reads

Structural evidence for a two-regime photobleaching mechanism in a reversibly switchable fluorescent protein.

J Am Chem Soc 2013 Oct 7;135(42):15841-50. Epub 2013 Oct 7.

Université Grenoble Alpes , Institut de Biologie Structurale (IBS), F-38027 Grenoble, France.

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http://dx.doi.org/10.1021/ja406860eDOI Listing
October 2013
30 Reads
6 Citations
12.113 Impact Factor

Revealing the excited-state dynamics of the fluorescent protein Dendra2.

J Phys Chem B 2013 Feb 15;117(8):2300-13. Epub 2013 Feb 15.

Division of Molecular Imaging and Photonics, Department of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200F, 3001 Heverlee, Belgium.

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http://dx.doi.org/10.1021/jp309219mDOI Listing
February 2013
11 Reads
4 Citations

Reversible photoswitching in fluorescent proteins: a mechanistic view.

IUBMB Life 2012 Jun 25;64(6):482-91. Epub 2012 Apr 25.

Pixel Team, IBS, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Université Joseph Fourier, Grenoble, France. dominique.bourgeois@ ibs.fr

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http://dx.doi.org/10.1002/iub.1023DOI Listing
June 2012
10 Reads
14 Citations
3.143 Impact Factor

Photoactivated structural dynamics of fluorescent proteins.

Biochem Soc Trans 2012 Jun;40(3):531-8

Pixel Team IBS, Institut de Biologie Structurale Jean-Pierre Ebel, Université Joseph Fourier, 41 rue Jules Horowitz, Grenoble, France.

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http://dx.doi.org/10.1042/BST20120002DOI Listing
June 2012
7 Reads
2 Citations
3.194 Impact Factor

The nature of transient dark states in a photoactivatable fluorescent protein.

J Am Chem Soc 2011 Nov 31;133(46):18586-9. Epub 2011 Oct 31.

Institut de Biologie Structurale (IBS)-Jean-Pierre Ebel, CEA/CNRS/ Université Joseph Fourier, 41, rue Jules Horowitz, 38027 Grenoble Cedex 1, France.

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http://dx.doi.org/10.1021/ja2085355DOI Listing
November 2011
6 Reads
5 Citations
12.113 Impact Factor

Rational design of photoconvertible and biphotochromic fluorescent proteins for advanced microscopy applications.

Chem Biol 2011 Oct;18(10):1241-51

Laboratory of Photochemistry and Spectroscopy, Department of Chemistry, Katholieke Universiteit Leuven, 3001 Heverlee, Belgium.

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http://dx.doi.org/10.1016/j.chembiol.2011.08.007DOI Listing
October 2011
16 Reads
20 Citations
6.645 Impact Factor

From EosFP to mIrisFP: structure-based development of advanced photoactivatable marker proteins of the GFP-family.

J Biophotonics 2011 Jun 14;4(6):377-90. Epub 2011 Feb 14.

National Oceanography Centre, University of Southampton, Southampton SO143ZH, UK.

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http://dx.doi.org/10.1002/jbio.201000122DOI Listing
June 2011
35 Reads
9 Citations
4.450 Impact Factor

Data storage based on photochromic and photoconvertible fluorescent proteins.

J Biotechnol 2010 Sep 21;149(4):289-98. Epub 2010 Apr 21.

Laboratory of Photochemistry and Spectroscopy, Department of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200F, 3001 Heverlee, Belgium.

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http://dx.doi.org/10.1016/j.jbiotec.2010.04.001DOI Listing
September 2010
8 Reads
5 Citations
2.871 Impact Factor

Low-temperature switching by photoinduced protonation in photochromic fluorescent proteins.

Photochem Photobiol Sci 2010 Feb 19;9(2):254-62. Epub 2010 Jan 19.

IBS, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, Université Joseph Fourier, 41 rue Jules Horowitz, F-38027, Grenoble, France.

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http://dx.doi.org/10.1039/b9pp00121bDOI Listing
February 2010
21 Reads
7 Citations
2.270 Impact Factor

Structural basis of X-ray-induced transient photobleaching in a photoactivatable green fluorescent protein.

J Am Chem Soc 2009 Dec;131(50):18063-5

European Synchrotron Radiation Facility, 6 rue Jules Horowitz, BP 220, 38043 Grenoble Cedex, France.

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http://dx.doi.org/10.1021/ja907296vDOI Listing
December 2009
74 Reads
20 Citations
12.113 Impact Factor

Photoconversion of the fluorescent protein EosFP: a hybrid potential simulation study reveals intersystem crossings.

J Am Chem Soc 2009 Nov;131(46):16814-23

CNRS, UMR5075, Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.

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http://dx.doi.org/10.1021/ja905380yDOI Listing
November 2009
8 Reads
3 Citations
12.113 Impact Factor

Cryophotolysis of a caged oxygen compound for use in low temperature biological studies.

Photochem Photobiol Sci 2009 Aug 1;8(8):1150-6. Epub 2009 Jun 1.

Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK OX1 3TA.

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http://dx.doi.org/10.1039/b821516bDOI Listing
August 2009
26 Reads
2 Citations
2.270 Impact Factor

Structural basis of enhanced photoconversion yield in green fluorescent protein-like protein Dendra2.

Biochemistry 2009 Jun;48(22):4905-15

European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, 8043 Grenoble Cedex, France.

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http://dx.doi.org/10.1021/bi900383aDOI Listing
June 2009
8 Reads
22 Citations
3.020 Impact Factor

Structural characterization of IrisFP, an optical highlighter undergoing multiple photo-induced transformations.

Proc Natl Acad Sci U S A 2008 Nov 18;105(47):18343-8. Epub 2008 Nov 18.

European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, 38043 Grenoble Cedex, France.

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http://dx.doi.org/10.1073/pnas.0805949105DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2587625PMC
November 2008
13 Reads
47 Citations
9.810 Impact Factor

Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.

Science 2007 Apr;316(5823):449-53

Institut de Biologie Structurale (IBS) Jean-Pierre Ebel, Commissariat à l'Energie Atomique (CEA), Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France.

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http://dx.doi.org/10.1126/science.1138885DOI Listing
April 2007
15 Reads
33 Citations
31.480 Impact Factor

Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide.

Proc Natl Acad Sci U S A 2006 Oct 25;103(40):14750-5. Epub 2006 Sep 25.

Département de Réponse et Dynamique Cellulaires/Laboratoire de Chimie et Biochimie des Centres Redox Biologiques, Unité Mixte de Recherche (UMR) 5047, CEA/CNRS, Université Joseph Fourier, 17 Avenue des Martyrs, 38054 Grenoble Cedex 9, France.

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http://dx.doi.org/10.1073/pnas.0510828103DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1595423PMC
October 2006
29 Reads
5 Citations
9.810 Impact Factor

The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition.

Biochemistry 2005 Jan;44(1):130-7

LCCP, UMR 5075, IBS-CEA/CNRS/UJF, 41 avenue Jules Horowitz, 38027 Grenoble Cedex 1, France.

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http://dx.doi.org/10.1021/bi0484163DOI Listing
January 2005
15 Reads
6 Citations
3.020 Impact Factor

Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction.

Structure 2004 Sep;12(9):1729-40

LCCP, UMR 5075, IBS-CEA/CNRS/Université J. Fourier, 41 Avenue Jules Horowitz, 38027 Grenoble, Cedex 1, France.

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http://dx.doi.org/10.1016/j.str.2004.07.013DOI Listing
September 2004
22 Reads
22 Citations
5.620 Impact Factor

A microspectrophotometer for UV–visible absorption and fluorescence studies of protein crystals

J. Appl. Cryst. 2002 Jun;35(3): 319-32

J Appl Cryst

Absorption microspectrophotometry has been shown to be of considerable help to probe crystalline proteins containing chromophores, metal centres, or coloured substrates/co-factors. Absorption spectra contribute to the proper interpretation of crystallographic structures, especially when transient intermediate states are studied. Here it is shown that fluorescence microspectrophotometry might also be used for such purposes if endogenous fluorophores are present in the macromolecule or when exogenous fluorophores are added and either bind to the protein or reside in the solvent channels. An off-line microspectrophotometer that is able to perform low-temperature absorption and fluorescence spectroscopy on crystals mounted in cryo-loops is described. One-shot steady-state emission spectra of outstanding quality were routinely collected from several samples. In some cases, crystals with optical densities that are too low or too high for absorption studies can still be tackled with fluorescence microspectrophotometry. The technique may be used for simple controls such as checking the presence, absence or redox state of a fluorescent substrate/co-factor. Potential applications in the field of kinetic crystallography are numerous. In addition, the possibility to probe key physico-chemical parameters of the crystal, such as temperature, pH or solvent viscosity, could trigger new studies in protein dynamics.

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December 2002
9 Reads

Top co-authors

Dominique Bourgeois
Dominique Bourgeois

Université Joseph Fourier

23
Martin Byrdin
Martin Byrdin

Université Grenoble Alpes

5
Johan Hofkens
Johan Hofkens

Katholieke Universiteit Leuven

4
Hideaki Mizuno
Hideaki Mizuno

Brain Science Institute

4
Benjamien Moeyaert
Benjamien Moeyaert

Katholieke Universiteit Leuven

3
Romain Berardozzi
Romain Berardozzi

Univ. Grenoble Alpes

3
Karin Nienhaus
Karin Nienhaus

University of Ulm

3
Philippe Carpentier
Philippe Carpentier

European Synchrotron Radiation Facility

3
Martin J Field
Martin J Field

Université Joseph Fourier

3