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DNA mapping in the capsid of giant bacteriophage phiEL (Caudovirales: Myoviridae: Elvirus) by analytical electron microscopy [Картирование ДНК в капсиде гигантского бактериофага phiEL (Caudovirales: Myoviridae: Elvirus) с помощью аналитической электронной микроскопии]
Trifonova T.S., Moiseenko A.V., Bourkaltseva M.V., Shaburova O.V., Shaytan A.K., Krylov V.N., Sokolova O.S.
, an inner body (IB) with supercoiled DNA molecule wrapped around it. Standard cryo-electron microscopy (cryo
Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF
Khusainov I., Vicens Q., Ayupov R., Usachev K., Myasnikov A., Simonetti A., Validov S., Kieffer B., Yusupova G., Yusupov M., Hashem Y.
(SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N
In vitro Reconstitution of the S. aureus 30S Ribosomal Subunit and RbfA Factor Complex for Structural Studies
Bikmullin A.G., Nurullina L.I., Garaeva N.S., Klochkova E.A., Blokhin D.S., Golubev A.A., Validov S.Z., Khusainov I.S., Usachev K.S., Yusupov M.M.
and optimization of the 30S–RbfA complex to obtain samples suitable for cryo-electron microscopy studies.
Differences in structure and hibernation mechanism highlight diversification of the microsporidian ribosome
Ehrenbolger K.
the cryo–electron microscopy structure of the ribosome from Paranosema locustae spores, bound
From structure of the complex to understanding of the biology
Rossmann M.G.
and is based on X-ray crystallography and on cryo-electron microscopy (cryo-EM) single-particle reconstructions
Картирование ДНК в капсиде гигантского бактериофага phiEL (Caudovirales: Myoviridae: Elvirus) с помощью аналитической электронной микроскопии
Трифонова Т.С., Моисеенко А.В., Буркальцева М.В., Шабурова О.В., Шайтан А.К., Крылов В.Н., Соколова О.С.
, an inner body (IB) with supercoiled DNA molecule wrapped around it. Standard cryo-electron microscopy (cryo
Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF
Khusainov I., Vicens Q., Ayupov R., Usachev K., Myasnikov A., Simonetti A., Validov S., Kieffer B., Yusupova G., Yusupov M., Hashem Y.
(SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N
Structural insights into plant viruses revealed by small-angle x-ray scattering and atomic force microscopy
Shtykova, E. V., Dubrovin, E. V., Ksenofontov, A. L., Gifer, P. K., Tokhtar, V. K.
spectroscopy and cryo-electron microscopy are well accepted methods to obtain the 3D protein structure
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism
Flygaard R., Boegholm N., Yusupov M., Jenner L.
structures of the T. thermophilus 100S ribosome determined by cryo-electron microscopy to average resolutions
Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance
Pellegrino S., Demeshkina N., Mancera-Martinez E., Melnikov S., Simonetti A., Myasnikov A., Yusupov M., Yusupova G., Hashem Y.
-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron

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