Natalia Maltseva
Papers
1
Total Citations
19
H-Index
1
About
Natalia Maltseva is a structural biologist whose work illuminates the hidden architecture of bacterial proteins. Her research centers on X-ray crystallography and the functional annotation of uncharacterized proteins, with a particular focus on pathogenic bacteria. Her most cited work, the 2006 paper "Crystal structure of hypothetical protein YfiH from *Shigella flexneri* at 2 Å resolution," has garnered 19 citations and stands as a cornerstone of her career. In this study, Maltseva solved the structure of the YfiH protein—a member of a vast, uncharacterized protein family—using the single wavelength anomalous dispersion (SAD) method. By determining the 2.01 Å resolution structure of this 243-residue protein from *Shigella flexneri* 2a str.2457T, she provided the first structural insights into a previously unknown protein family, laying the groundwork for future functional studies. Her achievement is notable for its technical rigor and its contribution to the broader goal of structural genomics: assigning function to the many "hypothetical" proteins encoded in bacterial genomes. Maltseva’s work exemplifies how structural biology can unlock the secrets of microbial pathogens.
Research Focus
Key Achievements
Top Papers
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