A5058504005- Enzyme Structure and Function
- RNA and protein synthesis mechanisms
- Protein Structure and Dynamics
- DNA and Nucleic Acid Chemistry
- Bacteriophages and microbial interactions
- Bacterial Genetics and Biotechnology
- Endoplasmic Reticulum Stress and Disease
- Enzyme Production and Characterization
- RNA modifications and cancer
- Biochemical and Molecular Research
- Glycosylation and Glycoproteins Research
- Rare-earth and actinide compounds
- Magnetic Properties of Alloys
- RNA Research and Splicing
- Advanced biosensing and bioanalysis techniques
- Ubiquitin and proteasome pathways
- Magnetic properties of thin films
- Photosynthetic Processes and Mechanisms
- Heat shock proteins research
- Microbial Metabolites in Food Biotechnology
- RNA Interference and Gene Delivery
- Cellular transport and secretion
- Metalloenzymes and iron-sulfur proteins
- Synthesis of Tetrazole Derivatives
- Synthesis and Characterization of Heterocyclic Compounds
Max Delbrück Center
2016-2025
Freie Universität Berlin
2013-2023
Beth Israel Deaconess Medical Center
2022
Harvard University
2022
Helmholtz Association of German Research Centres
2017
Max Planck Institute for Medical Research
2016
Charité - Universitätsmedizin Berlin
2012
Libin Cardiovascular Institute of Alberta
2012
University of Calgary
2012
Helmholtz Centre for Infection Research
2010
XDSAPP is a Tcl/Tk-based graphical user interface for the easy and convenient processing of diffraction data sets using XDS . It provides access to all functionalities, automates generates plots various set statistics provided by By incorporating additional software, further information on certain features set, such as radiation decay during collection or presence pseudo-translational symmetry and/or twinning, can be obtained. Intensity files suitable CCP4 , CNS SHELX are generated.
XDSAPP is an expert system and graphical user interface (GUI) for the automated processing of diffraction images using XDS program suite other programs. The latest major update extension are presented here. includes new features, as well improvements in GUI underlying decision-making system. freely available academic users.
The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved the transcriptional regulation at least two genes. shares high homology with nucleic acid-binding domain Y-box factors, family eukaryotic proteins and translational regulation. crystal structure CspA has been determined 2-A resolution refined to R = 0.187. composed five antiparallel beta-strands forming closed five-stranded beta-barrel. three-dimensional similar that...
A vector system is presented that allows generation of E. coli co-expression clones by a standardized, robust cloning procedure. The number co-expressed proteins not limited. Five 'pQLink' vectors for expression His-tag and GST-tag fusion as well untagged restriction enzymes or Gateway were generated. allow to be expressed individually; achieve co-expression, two pQLink plasmids are combined ligation-independent cloning. can accept an unrestricted genes. As example, the heterotetrameric...
The three-dimensional structure of the hybrid Bacillus 1,3-1,4-beta-glucanase (beta-glucanase; 1,3-1,4-beta-D-glucan 4-glucanohydrolase, lichenase, EC 3.2.1.73) designated H(A16-M) was determined by x-ray crystallography at a resolution 2.0 A and refined to an R value 16.4% using stereochemical restraints. protein molecule consists mainly two seven-stranded antiparallel beta-pleated sheets arranged atop each other form compact, sandwich-like structure. channel crossing one side accommodates...
The complex formed between the enzyme ribonuclease T1 (EC 3.1.27.3) and its specific inhibitor 2'-guanylic acid (2'-GMP) has been refined to R = 0.180 using x-ray diffraction data 1.9-A resolution. protein molecule displays a compact fold; 4.5 turn alpha-helix packed over an antiparallel beta-pleated sheet shields most of hydrophobic interior against solvent. extended pleated structure is composed three long four short strands building up two-stranded minor beta-sheet near amino terminus...
Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics. Bacillus subtilis biofilms contain TasA major proteinaceous component in addition to exopolysaccharides. In stark contrast the initially unfolded biofilm proteins of other bacteria, is a soluble, stably folded monomer, whose structure we have determined by X-ray crystallography. Subsequently, characterized vitro different oligomeric forms NMR, EM,...
Abstract The RNA-binding protein RC3H1 (also known as ROQUIN) promotes TNFα mRNA decay via a 3′UTR constitutive element (CDE). Here we applied PAR-CLIP to human identify ∼3,800 targets with >16,000 binding sites. A large number of sites are distinct from the consensus CDE and revealed structure-sequence motif U-rich sequences embedded in hairpins. binds preferentially short-lived DNA damage-induced mRNAs, indicating role this post-transcriptional regulation damage response. Intriguingly,...
The steroid hydroxylating system of adrenal cortex mitochondria consists the membrane-attached NADPH-dependent adrenodoxin reductase (AR), soluble one-electron transport protein (Adx), and a membrane-integrated cytochrome P450 CYP11 family. In 2.3-Å resolution crystal structure Adx·AR complex, 580 Å<sup>2</sup> partly polar surface are buried. Main interaction sites centered around Asp<sup>79</sup>, Asp<sup>76</sup>, Asp<sup>72</sup>, Asp<sup>39</sup> Adx Arg<sup>211</sup>,...
Sleeping Beauty (SB) is the most active Tc1/mariner-like transposon in vertebrate species. Each of terminal inverted repeats (IRs) SB contains two transposase-binding sites (DRs). This feature, termed IR/DR structure, conserved a group Tc1-like transposons. The DNA-binding region transposase, similar to paired domain Pax proteins, consists helix-turn-helix subdomains (PAI + RED = PAIRED). N-terminal PAI subdomain was found play dominant role contacting DRs. Transposase able bind mutant...
Abstract Proteins carry out the most important and difficult tasks in all living organisms. To do so, they must often interact specifically with other small large molecules. This requires that fold to a globular conformation unique active site is used for specific interaction. Consequently, protein folding can be regarded as “secret of life”. Biochemists chemists have great interest elucidating mechanism by which proteins predicting folded its stability given just amino acid sequence....