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Nature Structural & Molecular Biology|April 28, 2009
Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsisFang Fang Yin, Scott Bailey, C Axel Innis, et al.
Elife|July 26, 2018
Structural basis for potent and broad inhibition of HIV-1 RT by thiophene[3,2-d]pyrimidine non-nucleoside inhibitorsYang Yang, Dongwei Kang, Laura A Nguyen, et al.
Nature Structural & Molecular Biology|June 23, 2014
Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helixJessica A Brown, David Bulkley, Jimin Wang, et al.
Blood|January 27, 2009
The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding propertiesPaul R Stabach, Ivana Simonović, Miranda A Ranieri, et al.
Protein Science : a Publication of the Protein Society|September 30, 2017
On the relationship between cumulative correlation coefficients and the quality of crystallographic data setsJimin Wang, Gary W Brudvig, Victor S Batista, et al.
Acta Crystallographica. Section D, Structural Biology|April 7, 2021
Identification of Mg2+ ions next to nucleotides in cryo-EM maps using electrostatic potential mapsJimin Wang, S Kundhavai Natchiar, Peter B Moore, et al.
Molecular Cell|November 18, 2004
Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29Satwik Kamtekar, Andrea J Berman, Jimin Wang, et al.
The EMBO Journal|March 3, 2006
The phi29 DNA polymerase:protein-primer structure suggests a model for the initiation to elongation transitionSatwik Kamtekar, Andrea J Berman, Jimin Wang, et al.
Cell Reports|July 21, 2017
Crystal Structure of the Human Ribosome in Complex with DENR-MCT-1Ivan B Lomakin, Elena A Stolboushkina, Anand T Vaidya, et al.
Protein Science : a Publication of the Protein Society|September 23, 2018
On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiationJimin Wang, Zheng Liu, Robert H Crabtree, et al.
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