S'identifier

Bernard Lorber

Université de Strasbourg,
Architecture et Réactivité de l’ARN,
UPR 9002,
CNRS,
Université de Strasbourg, Architecture et Réactivité de l’ARN, UPR 9002, CNRS

Institut de Biologie Moléculaire et Cellulaire

BIOGRAPHY

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PUBLICATIONS

Comparative analysis of space-grown and earth-grown crystals of an aminoacyl-tRNA synthetase: space-grown crystals are more useful for structural determination.

Acta crystallographica. Section D, Biological crystallography Apr, 2002 | Pubmed ID: 11914489

Towards atomic resolution with crystals grown in gel: the case of thaumatin seen at room temperature.

Proteins Aug, 2002 | Pubmed ID: 12112683

Crystallization in the presence of glycerol displaces water molecules in the structure of thaumatin.

Acta crystallographica. Section D, Biological crystallography Dec, 2002 | Pubmed ID: 12454465

The crystallization of biological macromolecules under microgravity: a way to more accurate three-dimensional structures?

Biochimica et biophysica acta Sep, 2002 | Pubmed ID: 12479400

Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.

Acta crystallographica. Section D, Biological crystallography Jan, 2004 | Pubmed ID: 14684896

The transamidosome: a dynamic ribonucleoprotein particle dedicated to prokaryotic tRNA-dependent asparagine biosynthesis.

Molecular cell Oct, 2007 | Pubmed ID: 17964262

tRNA-dependent asparagine formation in prokaryotes: characterization, isolation and structural and functional analysis of a ribonucleoprotein particle generating Asn-tRNA(Asn).

Methods (San Diego, Calif.) Feb, 2008 | Pubmed ID: 18241796

Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon.

Journal of molecular biology Sep, 2008 | Pubmed ID: 18602926

Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.

The Journal of biological chemistry Jul, 2009 | Pubmed ID: 19443655

Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation.

Acta crystallographica. Section F, Structural biology and crystallization communications Jun, 2009 | Pubmed ID: 19478435

Reversible liposome association induced by LAH4: a peptide with potent antimicrobial and nucleic acid transfection activities.

Biophysical journal Jun, 2010 | Pubmed ID: 20513398

Crystal structure of the archaeal asparagine synthetase: interrelation with aspartyl-tRNA and asparaginyl-tRNA synthetases.

Journal of molecular biology Sep, 2011 | Pubmed ID: 21820443

The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code.

Nucleic acids research Jun, 2012 | Pubmed ID: 22362756

Protein analysis by dynamic light scattering: methods and techniques for students.

Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology Nov-Dec, 2012 | Pubmed ID: 23166025

Differential modes of peptide binding onto replicative sliding clamps from various bacterial origins.

Journal of medicinal chemistry Sep, 2014 | Pubmed ID: 25170813

Nanobody-mediated resistance to Grapevine fanleaf virus in plants.

Plant biotechnology journal 02, 2018 | Pubmed ID: 28796912

Interaction of a Model Peptide on Gram Negative and Gram Positive Bacterial Sliding Clamps.

ACS infectious diseases 06, 2019 | Pubmed ID: 30912430

A simple and versatile microfluidic device for efficient biomacromolecule crystallization and structural analysis by serial crystallography.

IUCrJ May, 2019 | Pubmed ID: 31098026

Structural Analysis of RNA by Small-Angle X-ray Scattering.

Methods in molecular biology (Clifton, N.J.) , 2020 | Pubmed ID: 32006316

Structural basis of nanobody recognition of grapevine fanleaf virus and of virus resistance loss.

Proceedings of the National Academy of Sciences of the United States of America 05, 2020 | Pubmed ID: 32371486

INSTITUTIONS

Institut de Biologie Moléculaire et Cellulaire

JOVE ARTICLES

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Raphaël de Wijn^1,4,

Kévin Rollet^1,2,

Vincent Olieric³,

Oliver Hennig²,

Nicola Thome¹,

Camille Noûs¹,

Caroline Paulus¹,

Bernard Lorber¹,

Heike Betat²,

Mario Mörl²,

Claude Sauter¹

¹Université de Strasbourg, Architecture et Réactivité de l’ARN, UPR 9002, CNRS, Institut de Biologie Moléculaire et Cellulaire,

²Biochemistry and Molecular Biology, Institute for Biochemistry, Leipzig University,

³, Paul Scherrer Institute, Swiss Light Source,

⁴, European XFEL GmbH

Biochemistry

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Bernard Lorber

.css-o250i3{font-size:18px;font-family:Open Sans,sans-serif;line-height:21.6px;}Université de Strasbourg,Architecture et Réactivité de l’ARN,UPR 9002,CNRS,Université de Strasbourg, Architecture et Réactivité de l’ARN, UPR 9002, CNRS

Institut de Biologie Moléculaire et Cellulaire

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip

Université de Strasbourg,
Architecture et Réactivité de l’ARN,
UPR 9002,
CNRS,
Université de Strasbourg, Architecture et Réactivité de l’ARN, UPR 9002, CNRS