ArticleProceedings of the National Academy of Sciences of the United States of America2004
Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange MS.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.Nature methods · 2019Review
- Glycosylation of viral surface proteins probed by mass spectrometry.Current opinion in virology · 2019Review
- Dynamic structural biology at the protein membrane interface.The Journal of biological chemistry · 2019Review
- Tracking Higher Order Protein Structure by Hydrogen-Deuterium Exchange Mass Spectrometry.Protein and peptide letters · 2019Review
- Dimerization interface of osteoprotegerin revealed by hydrogen-deuterium exchange mass spectrometry.The Journal of biological chemistry · 2018Article
- Article
- The repeat region of cortactin is intrinsically disordered in solution.Scientific reports · 2017Article
- Characterizing the Structure and Oligomerization of Major Royal Jelly Protein 1 (MRJP1) by Mass Spectrometry and Complementary Biophysical Tools.Biochemistry · 2017Article
- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- High Resolution Mapping of Bactericidal Monoclonal Antibody Binding Epitopes on Staphylococcus aureus Antigen MntC.PLoS pathogens · 2016Article
- Dynamics and architecture of the NRBF2-containing phosphatidylinositol 3-kinase complex I of autophagy.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Using hydrogen deuterium exchange mass spectrometry to engineer optimized constructs for crystallization of protein complexes: Case study of PI4KIIIβ with Rab11.Protein science : a publication of the Protein Society · 2016Article
- Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016Review
- Rare loss-of-function mutation in complement component C3 provides insight into molecular and pathophysiological determinants of complement activity.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.Molecular cell · 2015Article
- Assembly and dynamics of the autophagy-initiating Atg1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structures of PI4KIIIβ complexes show simultaneous recruitment of Rab11 and its effectors.Science (New York, N.Y.) · 2014Article
- DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.Nucleic acids research · 2014Article
5 more citing papers are in PubMed but not listed here.
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7 authors.
Funding
Abstract
Crystallographic efforts often fail to produce suitably diffracting protein crystals. Unstructured regions of proteins play an important role in this problem and considerable advantage can be gained in removing them. We have developed a number of enhancements to amide hydrogen/high-throughput and high-resolution deuterium exchange MS (DXMS) technology that allow rapid identification of unstructured regions in proteins. To demonstrate the utility of this approach for improving crystallization success, DXMS analysis was attempted on 24 Thermotoga maritima proteins with varying crystallization and diffraction characteristics. Data acquisition and analysis for 21 of these proteins was completed in 2 weeks and resulted in the localization and prediction of several unstructured regions within the proteins. When compared with those targets of known structure, the DXMS method correctly localized even small regions of disorder. DXMS analysis was then correlated with the propensity of such targets to crystallize and was further used to define truncations that improved crystallization. Truncations that were defined solely on DXMS analysis demonstrated greatly improved crystallization and have been used for structure determination. This approach represents a rapid and generalized method that can be applied to structural genomics or other targets in a high-throughput manner.
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