J
Jasmita Gill
Researcher at International Centre for Genetic Engineering and Biotechnology
Publications - 16
Citations - 201
Jasmita Gill is an academic researcher from International Centre for Genetic Engineering and Biotechnology. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 7, co-authored 7 publications receiving 167 citations.
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Journal ArticleDOI
Crystal Structure of Soluble Domain of Malaria Sporozoite Protein UIS3 in Complex with Lipid
TL;DR: The crystal structure of Plasmodium falciparum UIS3 soluble domain in complex with the lipid phosphatidylethanolamine (PE) provides a new target for abrogating parasite development within liver cells before typical symptoms of malaria can manifest.
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Crystal structure of malaria parasite nucleosome assembly protein distinct modes of protein localization and histone recognition
Jasmita Gill,Manickam Yogavel,Anuj Kumar,Hassan Belrhali,Sudhir Jain,Melanie Rug,Monica Brown,Alexander G. Maier,Amit Sharma +8 more
TL;DR: The crucial structural differences observed between parasite and yeast NAPs shed light on possible new modes of histone recognition by nucleosome assembly proteins.
Journal ArticleDOI
Structure of a superoxide dismutase and implications for copper-ion chelation.
Manickam Yogavel,Prakash Chandra Mishra,Jasmita Gill,Pardeep Kumar Bhardwaj,Som Dutt,Sanjay Kumar,Paramvir Singh Ahuja,Amit Sharma +7 more
TL;DR: This analysis provides new insights into the copper-chelation process in SODs and several new structural features in Pa-SOD which may be responsible for its unique properties of thermostability and expanded range of antioxidant activity are highlighted.
Journal ArticleDOI
Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum
Jasmita Gill,Anuj Kumar,Manickam Yogavel,Hassan Belrhali,Swatantra Kumar Jain,Melanie Rug,Monica Brown,Alexander G. Maier,Alexander G. Maier,Amit Sharma +9 more
TL;DR: Fluorescence spectroscopy data suggest that PfNapS interacts with core histones at a different site from its interaction with linker histone H1, and illustrates two regions on the Pf NapS dimer as the possible sites for histone recognition.
Journal ArticleDOI
SAD phasing of a structure based on cocrystallized iodides using an in-house Cu Kalpha X-ray source: effects of data redundancy and completeness on structure solution.
TL;DR: Cocrystallization of proteins with halide salts such as ammonium iodide in combination with copper-anode X-ray radiation can therefore serve as a powerful and easy avenue for structure solution.