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Biomedical subjects

G Illing

Publications and source records attributed to G Illing.

7 recordsLinked to original sources
PubMed2001

High-throughput three-dimensional protein structure determination.

In the wake of finished genomic sequencing projects, high-throughput analysis techniques are being developed in various fields of functional genomics. Of special interest in this regard is the three-dimensional structure analysis of proteins by X-ray crystallography and NMR spectroscopy, which has been characterized by distinctly low-throughput in the past. A number of recent advances in instrumentation and software are promising to radically change this situation, leaving the production of suitable protein samples as the sole rate-limiting step in structural analyses.

Crystallography, X-Ray↗
PubMed2000

An integrated approach to structural genomics.

Structural genomics aims at determining a set of protein structures that will represent all domain folds present in the biosphere. These structures can be used as the basis for the homology modelling of the majority of all remaining protein domains or, indeed, proteins. Structural genomics therefore promises to provide a comprehensive structural description of the protein universe. To achieve this, a broad scientific effort is required. The Berlin-based "Protein Structure Factory" (PSF) plans to contribute to this effort by setting up a local infrastructure for the low-cost, high-throughput analysis of soluble human proteins. In close collaboration with the German Human Genome Project (DHGP) protein-coding genes will be expressed in Escherichia coli or yeast. Affinity-tagged proteins will be purified semi-automatically for biophysical characterization and structure analysis by X-ray diffraction methods and NMR spectroscopy. In all steps of the structure analysis process, possibilities for automation, parallelization and standardization will be explored. Major new facilities that are created for the PSF include a robotic station for large-scale protein crystallization, an NMR center and an experimental station for protein crystallography at the synchrotron storage ring BESSY II in Berlin.

Crystallography, X-Ray↗
PubMed1996

Intravenous coronary angiography with dichromography using synchrotron radiation.

Dichromography represents a digital subtraction angiography mode based on energy substraction which allows imaging of fast moving subjects like the heart. For logarithmic subtraction 2 images with X-rays just below and above the iodine K-edge (33.17 keV) are simultaneously obtained in a line scan mode. Monochromatic X-rays of sufficient intensity to visualize coronary arteries of 1 mm diameter with extremely low iodine concentrations (1 mg/cm2) after venous injection is only provided by synchrotron radiation. The system NIKOS (non-invasive coronary arteriography with synchrotron radiation) at the Deutsches Elektronen Synchrotron (DESY) consists of 6 components: a wiggler, a monochromator, a safety system, a scanning device, a detector and a computer system. After experimental studies in dogs patients are imaged since 1990. Initial results demonstrate feasibility and safety of synchrotron radiation coronary angiography. Large scale studies are designed to further evaluate sensitivity and specificity. When compact synchrotron radiation sources become available, this technique could be used for follow-up studies and for evaluation of certain high coronary risk populations.

Angiography, Digital Subtraction↗
PubMed1992

Purification and properties of the RuvA and RuvB proteins of Escherichia coli.

The RuvA and RuvB proteins of Escherichia coli play important roles in the post-replicational repair of damaged DNA, genetic recombination and cell division. In this paper, we describe the construction of over expression vectors for RuvA and RuvB and detail simple purification schemes for each protein. The purified 22 kDa RuvA polypeptide forms a tetrameric protein (M(r) ca. 100,000) as observed by gel filtration. The tetramer is stabilised by strong disulphide bridges that resist denaturation during SDS-PAGE (in the absence of boiling and beta-mercaptoethanol). In contrast, purified RuvB polypeptides (37 kDa) weakly associate to form a dimeric protein (M(r) ca. 85,000). At low protein concentrations, the RuvB dimer dissociates into monomers. The multimeric forms of each protein may be covalently linked by the bifunctional cross-linking reagent dimethyl suberimidate. Addition of purified RuvA and RuvB to a RecA-mediated recombination reaction was found to stimulate the rate of strand exchange leading to the rapid formation of heteroduplex DNA.

Bacterial Proteins↗