Henning Stahlberg

Publication List Details

Period

1997 - 2006

Number

15

Co-Authors

Sulfur-bearing lipids for the covalent attachment of supported lipid bilayers to gold surfaces: a detailed characterization and analysis (2006)

Duschl, Claus, Liley, Martha, Lang, Holger, Ghandi, Azin, Zakeeruddin, Shaik M., Stahlberg, Henning, ...

In a recent paper, a new class of synthetic lipids, which self-assemble to form monolayers on gold surfaces, was introduced. The addn. of a monolayer of phospholipids to these layers results in...

The reaction center of the photounit of Rhodospirillum rubrum is anchored to the light-harvesting complex with four-fold rotational disorder (2006)

Stahlberg, Henning, Dubochet, Jacques, Vogel, Horst, Ghosh, Robin

The minimal photounit of the photosynthetic membranes of the purple non-sulfur bacterium Rhodospirillum rubrum, comprising the reaction center and the light-harvesting complex has been purified and...

Are the light-harvesting I complexes from Rhodospirillum rubrum arranged around the reaction center in a square geometry? (2006)

Stahlberg, Henning, Dubochet, Jacques, Vogel, Horst, Ghosh, Robin

The basic photosynthetic unit contg. the reaction center and the light-harvesting I complex (RC-LHI) of the purple non-sulfur bacterium Rhodospirillum rubrum was purified and reconstituted into...

Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits

Stahlberg, Henning, Kutejová, Eva, Suda, Kitaru, Wolpensinger, Bettina, Lustig, Ariel, Schatz, Gottfried, ...

Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible...

Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy

Nouwen, Nico, Stahlberg, Henning, Pugsley, Anthony P., Engel, Andreas

Secretins, a superfamily of multimeric outer membrane proteins, mediate the transport of large macromolecules across the outer membrane of Gram-negative bacteria. Limited proteolysis of secretin PulD...

Bacterial Na+-ATP synthase has an undecameric rotor

Stahlberg, Henning, Müller, Daniel J., Suda, Kitaru, Fotiadis, Dimitrios, Engel, Andreas, Meier, Thomas, ...

Synthesis of adenosine triphosphate (ATP) by the F1F0 ATP synthase involves a membrane-embedded rotary engine, the F0 domain, which drives the extra-membranous catalytic F1 domain. The F0 domain...

The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer

Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, ...

GlpF, the glycerol facilitator protein of Escherichia coli, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine-tagged protein was overexpressed,...

Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits

Stahlberg, Henning, Kutejová, Eva, Suda, Kitaru, Wolpensinger, Bettina, Lustig, Ariel, Schatz, Gottfried, ...

Lon (or La) is a soluble, homooligomeric ATP-dependent protease. Mass determination and cryoelectron microscopy of pure mitochondrial Lon from Saccharomyces cerevisiae identify Lon as a flexible...

Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy

Nouwen, Nico, Stahlberg, Henning, Pugsley, Anthony P., Engel, Andreas

Secretins, a superfamily of multimeric outer membrane proteins, mediate the transport of large macromolecules across the outer membrane of Gram-negative bacteria. Limited proteolysis of secretin PulD...

Bacterial Na+-ATP synthase has an undecameric rotor

Stahlberg, Henning, Müller, Daniel J., Suda, Kitaru, Fotiadis, Dimitrios, Engel, Andreas, Meier, Thomas, ...

Synthesis of adenosine triphosphate (ATP) by the F1F0 ATP synthase involves a membrane-embedded rotary engine, the F0 domain, which drives the extra-membranous catalytic F1 domain. The F0 domain...

The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer

Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, ...

GlpF, the glycerol facilitator protein of Escherichia coli, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine-tagged protein was overexpressed,...

Functional modulation of IFT kinesins extends the sensory repertoire of ciliated neurons in Caenorhabditis elegans

Evans, James E., Snow, Joshua J., Gunnarson, Amy L., Ou, Guangshuo, Stahlberg, Henning, McDonald, Kent L., ...

The diversity of sensory cilia on Caenorhabditis elegans neurons allows the animal to detect a variety of sensory stimuli. Sensory cilia are assembled by intraflagellar transport (IFT) kinesins,...