ArticleProceedings of the National Academy of Sciences of the United States of America2005
NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 88 citations in OpenAlex.
- PDZ Sample Quality Assessment by Biochemical and Biophysical Characterizations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Insights into Structures and Dynamics of Flavivirus Proteases from NMR Studies.International journal of molecular sciences · 2020Review
- A structural study of the complex between neuroepithelial cell transforming gene 1 (Net1) and RhoA reveals a potential anticancer drug hot spot.The Journal of biological chemistry · 2018Article
- Differential reactivity of closely related zinc(II)-binding metallothioneins from the plant Arabidopsis thaliana.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome.Scientific reports · 2016Article
- Application of data mining tools for classification of protein structural class from residue based averaged NMR chemical shifts.Biochimica et biophysica acta · 2015Article
- Biophysical Studies on BEX3, the p75NTR-Associated Cell Death Executor, Reveal a High-Order Oligomer with Partially Folded Regions.PloS one · 2015Article
- Intrinsically disordered regions in autophagy proteins.Proteins · 2014Article
- Protein production for structural genomics using E. coli expression.Methods in molecular biology (Clifton, N.J.) · 2014Article
- NMR-profiles of protein solutions.Biopolymers · 2013Article
- Electrospray ionization-induced protein unfolding.Journal of the American Society for Mass Spectrometry · 2012Article
- The J-UNIO protocol for automated protein structure determination by NMR in solution.Journal of biomolecular NMR · 2012Article
- Article
- Of bits and bugs--on the use of bioinformatics and a bacterial crystal structure to solve a eukaryotic repeat-protein structure.PloS one · 2010Article
- Prediction of protein crystallization outcome using a hybrid method.Journal of structural biology · 2010Article
- Rapid, robotic, small-scale protein production for NMR screening and structure determination.Protein science : a publication of the Protein Society · 2010Article
- Benefits of structural genomics for drug discovery research.Infectious disorders drug targets · 2009Review
- CSSI-PRO: a method for secondary structure type editing, assignment and estimation in proteins using linear combination of backbone chemical shifts.Journal of biomolecular NMR · 2009Article
- High-throughput screening of optimal solution conditions for structural biological studies by fluorescence correlation spectroscopy.Protein science : a publication of the Protein Society · 2009Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
In the Joint Center for Structural Genomics, one-dimensional (1D) 1H NMR spectroscopy is routinely used to characterize the folded state of protein targets and, thus, serves to guide subsequent crystallization efforts and to identify proteins for NMR structure determination. Here, we describe 1D 1H NMR screening of a group of 79 mouse homologue proteins, which correlates the NMR data with the outcome of subsequent crystallization experiments and crystallographic structure determination. Based on the 1D 1H NMR spectra, the proteins are classified into four groups, "A" to "D." A-type proteins are candidates for structure determination by NMR or crystallography; "B"-type are earmarked for crystallography; "C" indicates folded globular proteins with broadened line shapes; and "D" are nonglobular, "unfolded" polypeptides. The results obtained from coarse- and fine-screen crystallization trials imply that only A- and B-type proteins should be used for extensive crystallization trials in the future, with C and D proteins subjected only to coarse-screen crystallization trials. Of the presently studied 79 soluble protein targets, 63% yielded A- or B-quality 1D 1H NMR spectra. Although similar yields of crystallization hits were obtained for all four groups, A to D, crystals from A- and B-type proteins diffracted on average to significantly higher resolution than crystals produced from C- or D-type proteins. Furthermore, the output of refined crystal structures from this test set of proteins was 4-fold higher for A- and B-type than for C- and D-type proteins.
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