J
John K. Everett
Researcher at Rutgers University
Publications - 14
Citations - 1217
John K. Everett is an academic researcher from Rutgers University. The author has contributed to research in topics: Structural genomics & Protein Data Bank. The author has an hindex of 13, co-authored 14 publications receiving 1095 citations. Previous affiliations of John K. Everett include Structural Genomics Consortium & Center for Advanced Biotechnology and Medicine.
Papers
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Journal ArticleDOI
Codon influence on protein expression in E. coli correlates with mRNA levels
Grégory Boël,Grégory Boël,Reka Letso,Helen Neely,W. Nicholson Price,W. Nicholson Price,Kam Ho Wong,Min Su,Jon D. Luff,Mayank Valecha,John K. Everett,Thomas Acton,Rong Xiao,Gaetano T. Montelione,Daniel P. Aalberts,John F. Hunt +15 more
TL;DR: The results suggest that codon content modulates a kinetic competition between protein elongation and mRNA degradation that is a central feature of the physiology and also possibly the regulation of translation in E. coli.
Journal ArticleDOI
Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data
W. Nicholson Price,W. Nicholson Price,Yang Chen,Samuel K. Handelman,Samuel K. Handelman,Helen Neely,Philip C. Manor,Richard Karlin,Rajesh Nair,Jinfeng Liu,Michael Baran,Michael Baran,John K. Everett,John K. Everett,Saichiu N Tong,Saichiu N Tong,Farhad Forouhar,Swarup S Swaminathan,Thomas Acton,Thomas Acton,Rong Xiao,Rong Xiao,Joseph R. Luft,Joseph R. Luft,Angela Lauricella,Angela Lauricella,George T. DeTitta,George T. DeTitta,Burkhard Rost,Gaetano T. Montelione,Gaetano T. Montelione,Gaetano T. Montelione,John F. Hunt +32 more
TL;DR: The analysis of large-scale experimental results of the Northeast Structural Genomics Consortium and experimental folding studies leads to the conclusion that crystallization propensity depends primarily on the prevalence of well-ordered surface epitopes capable of mediating interprotein interactions and is not strongly influenced by overall thermodynamic stability.
Book ChapterDOI
Robotic Cloning and Protein Production Platform of the Northeast Structural Genomics Consortium
Thomas Acton,Kristin C. Gunsalus,Rong Xiao,Li Chung Ma,James M. Aramini,Michael Baran,Yi Wen Chiang,Teresa Climent,Bonnie Cooper,Natalia G. Denissova,Shawn M. Douglas,John K. Everett,Chi K. Ho,Daphne Macapagal,P.K. Rajan,Ritu Shastry,Liang-Yu Shih,G.V.T. Swapna,Michael Wilson,Margaret Wu,Mark Gerstein,Masayori Inouye,John F. Hunt,Gaetano T. Montelione +23 more
TL;DR: The methods described here have proven effective in producing quality samples of both eukaryotic and prokaryotic proteins and will be of broad value to the structural biology, functional proteomics, and structural genomics communities.
Journal ArticleDOI
The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium
Rong Xiao,Stephen Anderson,James M. Aramini,R.L. Belote,W.A. Buchwald,Colleen Ciccosanti,Ken Conover,John K. Everett,Keith Hamilton,Yuanpeng J. Huang,Haleema Janjua,Mei Jiang,G. Kornhaber,D. Lee,Jessica Y. Locke,Li Chung Ma,Melissa Maglaqui,Lei Mao,Saheli Mitra,Dayaban Patel,Paolo Rossi,Seema Sahdev,Seema Sharma,Ritu Shastry,G. V. T. Swapna,Saichu N. Tong,Dongyan Wang,Huang Wang,Li Zhao,Gaetano T. Montelione,Thomas Acton +30 more
TL;DR: The core Protein Production Platform of the Northeast Structural Genomics Consortium (NESG) is described and the strategies used for producing high-quality protein samples are outlined, centered on the cloning, expression and purification of 6X-His-tagged proteins using T7-based Escherichia coli systems.
Journal ArticleDOI
A microscale protein NMR sample screening pipeline
Paolo Rossi,Paolo Rossi,G. V. T. Swapna,G. V. T. Swapna,Yuanpeng J. Huang,Yuanpeng J. Huang,James M. Aramini,James M. Aramini,Clemens Anklin,K. Conover,K. Conover,Keith Hamilton,Keith Hamilton,Rong Xiao,Rong Xiao,Thomas Acton,Thomas Acton,Asli Ertekin,Asli Ertekin,John K. Everett,John K. Everett,Gaetano T. Montelione,Gaetano T. Montelione +22 more
TL;DR: The overall process used by the NESG for screening NMR samples as part of a sample optimization process, assessing optimal construct design and solution conditions, as well as for determining protein rotational correlation times in order to assess protein oligomerization states is described.