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Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens
Related publications (36)
Miniaturized Sample Preparation for Transmission Electron Microscopy
Henning Paul-Julius Stahlberg, Anastasia Syntychaki
Due to recent technological progress, cryo-electron microscopy (cryo-EM) is rapidly becoming a standard method for the structural analysis of protein complexes to atomic resolution. However, protein isolation techniques and sample preparation methods for E ...
MyJove Corporation2018Focus: The interface between data collection and data processing in cryo-EM
We present a new software package called Focus that interfaces cryo-transmission electron microscopy (cryo-EM) data collection with computer image processing. Focus creates a user-friendly environment to import and manage data recorded by direct electron d ...
Elsevier BV2017Cryo-EM reconstruction of Type VI secretion system baseplate and sheath distal end
Henning Paul-Julius Stahlberg, Sergey Nazarov
The bacterial Type VI secretion system (T6SS) assembles from three major parts: a membrane complex that spans inner and outer membranes, a baseplate, and a sheath-tube polymer. The baseplate assembles around a tip complex with associated effectors and conn ...
EMBO2017High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer
Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium ...
Elsevier BV2017Total Sample Conditioning and Preparation of Nanoliter Volumes for Electron Microscopy
Electron microscopy (EM) entered a new era with the emergence of direct electron detectors and new nanocrystal electron diffraction methods. However, sample preparation techniques have not progressed and still suffer from extensive blotting steps leading t ...
American Chemical Society (ACS)2016X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form
beta-Barrel pore-forming toxins (beta-PFT), a large family of bacterial toxins, are generally secreted as water-soluble monomers and can form oligomeric pores in membranes following proteolytic cleavage and interaction with cell surface receptors. Monalysi ...
American Society for Biochemistry and Molecular Biology20153D reconstruction of two-dimensional crystals
Henning Paul-Julius Stahlberg, Andreas Engel
Electron crystallography of two-dimensional (2D) crystals determines the structure of membrane proteins in the lipid bilayer by imaging with cryo-electron microscopy and image processing. Membrane proteins can be packed in regular 2D arrays by their recons ...
Elsevier BV2015Exploring the Interactome: Microfluidic Isolation of Proteins and Interacting Partners for Quantitative Analysis by Electron Microscopy
Multimolecular protein complexes are important for many cellular processes. However, the stochastic nature of the cellular interactome makes the experimental detection of complex protein assemblies difficult and quantitative analysis at the single molecule ...
American Chemical Society (ACS)2014Cryo-electron microscopy of membrane proteins
Electron crystallography is used to study membrane proteins in the form of planar, two-dimensional (2D) crystals, or other crystalline arrays such as tubular crystals. This method has been used to determine the atomic resolution structures of bacteriorhodo ...
Humana Press2013Structure of the Dodecameric Yersinia enterocolitica Secretin YscC and Its Trypsin-Resistant Core
Henning Paul-Julius Stahlberg, Andreas Engel
The type Ill secretion system machinery, also known as the injectisome, delivers bacterial effector proteins into eukaryotic cells during infection. The outer membrane YscC secretin is a major part of Yersinia enterocolitica's injectisome and is among the ...
Elsevier BV2013