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Andrey Krasilnikov

Professor of Biochemistry and Molecular Biology
Image of Andrey Krasilnikov

Department of University Committees

  • Peer Teaching Evaluation

  • Curricular Affairs and Assessment

  • Commencement



Program or Departmental Affiliations

The BMMB Graduate Program




The Center for RNA Biology


Research Interest

Structural biology of RNA and RNA-protein complexes



Honors and Awards


Degree Cum Laude, Moscow Institute of Physics and Technology


Russian State Fellowship for Young Scientists, The Government of Russian Federation


National Research Service Award, National Institutes of Health


Beckman Young Investigator Award, Beckman Foundation


Basil O’Connor Scholar Research Award, March of Dimes Foundation (declined)


National Scientist Development Grant, American Heart Association


Daniel R. Tershak Award for Excellence in Teaching, Penn State University



Selected Publications

  • Perederina A, Li D, Lee H, Bator C, Berezin I, Hafenstein SL, Krasilnikov AS (2020). Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP. Nature Communications 11: 3474.
  • Perederina A, Berezin I, Krasilnikov AS (2018). In vitro reconstitution and analysis of eukaryotic RNase P RNPs. Nucleic Acids Research 46: 6857-6868.
  • Gopalan V, Jarrous N, Krasilnikov AS (2018). Change and necessity in the evolution of RNase P. RNA 24: 1-5.
  • Lemieux B, Laterreur N, Perederina A, Noel J-F, Dubois M-L, Krasilnikov AS, Wellinger RJ (2016). Active yeast telomerase shares subunits with ribonucleoproteins RNase P and RNase MRP. Cell 165: 1171-1181.
  • Fagerlund RD, Perederina A, Berezin I, Krasilnikov AS (2015). Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components. RNA21: 1591-1605.
  • Krasilnikov AS (2014). Applying UV-crosslinking to study RNA-protein interactions in multicomponent ribonucleoprotein complexes. Methods Mol. Biol. 1086: 193-207.
  • Esakova O, Perederina A, Berezin I, Krasilnikov AS (2013). Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate. Nucleic Acids Research 41: 7084-7091.
  • Khanova E, Esakova O, Perederina A, Berezin I, Krasilnikov AS (2012). Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions. RNA 18: 720-728.
  • Perederina A, Krasilnikov AS (2012). Crystallization of RNA-protein complexes: from synthesis and purification of individual components to crystals. Methods Mol. Biol. 905: 123-143.
  • Perederina A, Khanova E, Quan C, Berezin I, Esakova O, Krasilnikov AS (2011). Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. RNA 17: 1922-1931.
  • Krasilnikov AS (2011). Ribonucleoprotein ribonucleases P and MRP. In Ribonucleases (ed. Nicholson AW), pp 319-342. Springer, New York, NY, doi: 10.1007/978-3-642-21078-5_13
  • Esakova O, Perederina A, Quan C, Berezin I, Krasilnikov AS (2011). Substrate recognition by ribonucleoprotein Ribonuclease MRP. RNA 17: 356-364.
  • Esakova O, Krasilnikov AS (2010). Of proteins and RNA: the RNase P/MRP family. RNA 16: 1725-1747.
  • Perederina A, Krasilnikov AS (2010). The P3 domain of eukaryotic RNases P/MRP: Making a protein-rich RNA-based enzyme. RNA Biology 7: 534-539.
  • Perederina A, Esakova O, Quan, C, Khanova E, Krasilnikov AS (2010). Eukaryotic Ribonucleases P/MRP: the crystal structure of the P3 domain. EMBO J. 29: 761-769.
  • Lu Q, Wierzbicki S, Krasilnikov AS, Schmitt ME (2010). Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components. RNA 16: 529-537.
  • Perederina A, Esakova O, Quan C, Khanova E, Krasilnikov AS (2010). Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast Ribonuclease MRP in a complex with RNase P/ MRP protein components Pop6 and Pop7. Acta Crystallographica F66: 76-80.
  • Esakova O, Perederina A, Quan C, Schmitt ME, Krasilnikov AS (2008). Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes. RNA14: 1558-1567.
  • Perederina A, Esakova O, Koc H, Schmitt ME, Krasilnikov AS (2007). Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of yeast RNase MRP and RNase P RNAs. RNA 13: 1648-1655.
  • Baird NJ, Srividya N, Krasilnikov AS, Mondragon A, Sosnick TR, Pan T (2006). Structural basis for altering the stability of homologous RNAs from a mesophilic and a thermophilic bacterium. RNA 12: 598-606.
  • Torres-Larios A, Swinger, KK, Krasilnikov AS, Pan T, Mondragon A (2005). Crystal structure of the RNA component of bacterial Ribonuclease P. Nature 437: 584-587.
  • Krasilnikov AS, Xiao Y, Pan T, Mondragon A (2004). Basis for structural diversity in homologous RNAs. Science 306: 104-107.
  • Krasilnikov AS, Mondragon A (2003). On the occurrence of the T-loop RNA folding motif in large RNA molecules. RNA 9:640-643.
  • Krasilnikov AS, Yang XJ, Pan T, Mondragon A (2003). Crystal structure of the specificity domain of ribonuclease P. Nature 421: 760-764.