title: High-throughput three-dimensional protein structure determination.
abstract: 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.
authors.affiliation: Forschungsgruppe Kristallographie, Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, D-13125 Berlin, Germany. heinemann@mdc-berlin.de
authors.forename: U
authors.initials: U
authors.lastname: Heinemann
authors.forename: G
authors.initials: G
authors.lastname: Illing
authors.forename: H
authors.initials: H
authors.lastname: Oschkinat
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D008164:Luminescent Proteins; D049452:Green Fluorescent Proteins