Abstract
Contact and support
Need help, have a question, or want to contact the ResearchHub team?
© 2026 ResearchHub. Built for responsible scholarly connection.
Samantha J. Ziegler, Sam J. B. Mallinson, Peter C. St. John, Yannick J. Bomble
Abstract
Authors
Institutions
Provenance
crossref
Confidence 100%
pubmed
Confidence 98%
europepmc
Confidence 96%
openalex
No local reference links have been materialized yet.
10.1073/pnas.79.10.3236
10.1073/pnas.79.10.3236
10.1002/pro.3092
10.1002/pro.3092
High-throughput protein purification and quality assessment for crystallization
10.1016/j.ymeth.2011.07.010 · 2011
10.1038/nprot.2013.116
10.1038/nprot.2013.116
10.1126/science.1127344
10.1126/science.1127344
10.1016/j.ymeth.2017.01.005
10.1016/j.ymeth.2017.01.005
10.1126/science.1228565
10.1126/science.1228565
Integrative approaches in structural biology: a more complete picture from the combination of individual techniques
10.3390/biom9080370 · 2019
10.1016/j.ymeth.2019.03.009
10.1016/j.ymeth.2019.03.009
Structure of myoglobin: a three-dimensional Fourier synthesis at 2 A. resolution
10.1038/185422a0 · 1960
10.1107/97809553602060000822
10.1107/97809553602060000822
Confidence 95%
unpaywall
Confidence 95%
doaj
Confidence 92%
datacite
Confidence 0%
EIGER detector: application in macromolecular crystallography
10.1107/s2059798316012304 · 2016
10.1016/j.str.2004.03.011
10.1016/j.str.2004.03.011
Introduction to phasing
10.1107/s0907444910006694 · 2010
10.1107/s1600577515016604
10.1107/s1600577515016604
10.1107/s0907444911007773
10.1107/s0907444911007773
10.1107/s0021889809045701
10.1107/s0021889809045701
VMXi: a fully automated, fully remote, high-flux in situ macromolecular crystallography beamline
10.1107/s1600577518015114 · 2019
10.1107/s2059798316001078
10.1107/s2059798316001078
10.1073/pnas.1814526116
10.1073/pnas.1814526116
10.1038/nature09750
10.1038/nature09750
The nuclear induction experiment
10.1103/physrev.70.474 · 1946
10.1063/1.1719961
10.1063/1.1719961
Two-dimensional spectroscopy
1976
10.1021/ja00186a066
10.1021/ja00186a066
10.1016/0009-2614(80)80041-8
10.1016/0009-2614(80)80041-8
10.1139/v70-184
10.1139/v70-184
10.1063/1.1733605
10.1063/1.1733605
10.1126/science.278.5340.1111
10.1126/science.278.5340.1111
Protein dynamics and function from solution state NMR spectroscopy
10.1017/s0033583516000019 · 2016
10.1016/j.bbagen.2014.12.003
10.1016/j.bbagen.2014.12.003
10.1002/pro.2081
10.1002/pro.2081
10.1073/pnas.2002598117
10.1073/pnas.2002598117
10.1007/s12038-016-9640-y
10.1007/s12038-016-9640-y
Nuclear magnetic resonance (NMR) applied to membrane-protein complexes
10.1017/s003358351600010x · 2016
10.1016/j.bbapap.2017.07.004
10.1016/j.bbapap.2017.07.004
Protein Structure Determination in Living Cells
10.3390/ijms20102442 · 2019
10.1039/c7an01635b
10.1039/c7an01635b
In-cell NMR: a topical review
10.1107/s2052252516020625 · 2017
10.1016/j.jsb.2010.06.012
10.1016/j.jsb.2010.06.012
10.1021/jasms.9b00085
10.1021/jasms.9b00085 · doi-reference
10.1021/acs.analchem.9b02372
10.1021/acs.analchem.9b02372 · doi-reference
10.1021/acs.jproteome.7b00068
10.1021/acs.jproteome.7b00068 · doi-reference
Systems structural biology measurements by in vivo cross-linking with mass spectrometry
10.1038/s41596-019-0181-3 · doi-reference
Capturing protein communities by structural proteomics in a thermophilic eukaryote
10.15252/msb.20167412 · doi-reference
10.1021/acs.jproteome.9b00447
10.1021/acs.jproteome.9b00447 · doi-reference
10.1016/j.jsb.2013.06.012
10.1016/j.jsb.2013.06.012 · doi-reference
10.1016/j.jsb.2016.11.002
10.1016/j.jsb.2016.11.002 · doi-reference
Evolution of higher torque in Campylobacter-type bacterial flagellar motors
10.1038/s41598-017-18115-1 · doi-reference
10.1038/nmicrobiol.2017.59
10.1038/nmicrobiol.2017.59 · doi-reference
10.1126/science.aaf9620
10.1126/science.aaf9620 · doi-reference
10.15252/embr.201744261
10.15252/embr.201744261 · doi-reference
10.1016/j.jmb.2016.01.004
10.1016/j.jmb.2016.01.004 · doi-reference
10.1016/bs.mie.2016.04.014
10.1016/bs.mie.2016.04.014 · doi-reference
10.1146/annurev-biochem-061516-044741
10.1146/annurev-biochem-061516-044741 · doi-reference
10.1016/j.tcb.2016.08.006
10.1016/j.tcb.2016.08.006 · doi-reference
10.1021/acs.analchem.7b04431
10.1021/acs.analchem.7b04431 · doi-reference
Designs and applications of fluorescent protein-based biosensors
10.1016/j.cbpa.2009.09.033 · doi-reference
10.1016/j.str.2018.03.011
10.1016/j.str.2018.03.011 · doi-reference
10.1038/nature26003
10.1038/nature26003 · doi-reference
10.1016/j.cell.2020.02.058
10.1016/j.cell.2020.02.058 · doi-reference
10.1006/jmbi.2001.4644
10.1006/jmbi.2001.4644 · doi-reference
10.1002/pro.2206
10.1002/pro.2206 · doi-reference
10.1016/j.jsb.2019.07.004
10.1016/j.jsb.2019.07.004 · doi-reference
Yosshi: a web-server for disulfide engineering by bioinformatic analysis of diverse protein families
10.1093/nar/gkz385 · doi-reference
10.1093/protein/2.2.119
10.1093/protein/2.2.119 · doi-reference
10.1093/proeng/gzg024
10.1093/proeng/gzg024 · doi-reference
Disulfide by Design 2.0: a web-based tool for disulfide engineering in proteins
10.1186/1471-2105-14-346 · doi-reference
Benchmarking and analysis of protein docking performance in Rosetta v3.2
10.1371/journal.pone.0022477 · doi-reference
DOT2: Macromolecular docking with improved biophysical models
10.1002/jcc.23304 · doi-reference
10.1093/bioinformatics/btu097
10.1093/bioinformatics/btu097 · doi-reference
10.1021/acs.jctc.7b00125
10.1021/acs.jctc.7b00125 · doi-reference
10.1083/jcb.201112098
10.1083/jcb.201112098 · doi-reference
10.1016/j.sbi.2015.10.006
10.1016/j.sbi.2015.10.006 · doi-reference
10.1128/mr.59.1.94-123.1995
10.1128/mr.59.1.94-123.1995 · doi-reference
Network-based prediction of protein interactions
10.1038/s41467-019-09177-y · doi-reference
Multimodal deep representation learning for protein interaction identification and protein family classification
10.1186/s12859-019-3084-y · doi-reference
Predicting protein-protein interactions from matrix-based protein sequence using convolution neural network and feature-selective rotation forest
10.1038/s41598-019-46369-4 · doi-reference
10.1016/j.jmb.2007.05.022
10.1016/j.jmb.2007.05.022 · doi-reference
10.1093/bioinformatics/bti366
10.1093/bioinformatics/bti366 · doi-reference