Combining Electron Microscopy (EM) and Cross-Linking Mass Spectrometry (XL-MS) for Structural Characterization of Protein Complexes

2021 ◽  
pp. 217-232
Author(s):  
Lucía Quintana-Gallardo ◽  
Moisés Maestro-López ◽  
Jaime Martín-Benito ◽  
Miguel Marcilla ◽  
Daniel Rutz ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Mass Spectrometry ◽  
Structural Characterization ◽  
Protein Complexes ◽  
Cross Linking

Characterization of In Vivo Protein Complexes via Chemical Cross-Linking and Mass Spectrometry

2021 ◽  
Author(s):  
Yuefan Wang ◽  
Yingwei Hu ◽  
Naseruddin Höti ◽  
Lan Huang ◽  
Hui Zhang
Keyword(s):  
Mass Spectrometry ◽  
Protein Complexes ◽  
Cross Linking ◽  
Chemical Cross Linking

scholarly journals Structural Characterization of Native Proteins and Protein Complexes by Electron Ionization Dissociation-Mass Spectrometry

2017 ◽  
Vol 89 (5) ◽  
pp. 2731-2738 ◽  
Author(s):  
Huilin Li ◽  
Yuewei Sheng ◽  
William McGee ◽  
Michael Cammarata ◽  
Dustin Holden ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structural Characterization ◽  
Protein Complexes ◽  
Electron Ionization ◽  
Native Proteins

scholarly journals Driving Integrative Structural Modeling with Serial Capture Affinity Purification

2020 ◽  
Author(s):  
Xingyu Liu ◽  
Ying Zhang ◽  
Zhihui Wen ◽  
Yan Hao ◽  
Charles A.S. Banks ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structural Model ◽  
Protein Complexes ◽  
Affinity Purification ◽  
Quantitative Imaging ◽  
Specific Protein ◽  
Cross Linking ◽  
Affinity Enrichment

AbstractStreamlined characterization of protein complexes remains a challenge for the study of protein interaction networks. Here, we describe Serial Capture Affinity Purification (SCAP) where two separate proteins are tagged with either the HaloTag or the SNAP-tag, permitting a multi-step affinity enrichment of specific protein complexes. The multifunctional capabilities of these protein tagging systems also permit in vivo validation of interactions using FRET and FCCS quantitative imaging. When coupling SCAP to cross-linking mass spectrometry, an integrated structural model of the complex of interest can be generated. We demonstrate this approach using the Spindlin1 and SPINDOC chromatin associated protein complex, culminating in a structural model with two SPINDOC docked on one SPIN1 molecule. In this model, SPINDOC interacts with the SPIN1 interface previously shown to bind a lysine and arginine methylated sequence of histone H3 Taken together, we present an integrated affinity purification, live cell imaging, and cross linking mass spectrometry approach for the building of integrative structural models of protein complexes.

Structural characterization of chelator-terminated dendrimers and their synthetic intermediates by mass spectrometry

2005 ◽  
Vol 40 (9) ◽  
pp. 1203-1214 ◽  
Author(s):  
Ursula E. Ch. Berndt ◽  
Tao Zhou ◽  
Robert C. Hider ◽  
Zu D. Liu ◽  
Hendrik Neubert
Keyword(s):  
Mass Spectrometry ◽  
Structural Characterization ◽  
Synthetic Intermediates
Sign in / Sign up

Export Citation Format

Share Document