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@BOOK{Lucas:472123,
      author       = {Gisriel, Christopher and Fromme, Petra and Martin-Garcia,
                      Jose M.},
      editor       = {Lucas, Alexandra R.},
      title        = {{M}ethods for {C}rystallization and {S}tructural
                      {D}etermination of {M}-{T}7 {P}rotein from {M}yxoma {V}irus},
      volume       = {2225},
      address      = {New York, NY},
      publisher    = {Springer},
      reportid     = {PUBDB-2021-04846},
      isbn         = {978-1-0716-1011-4 (print)},
      series       = {Methods in Molecular Biology},
      pages        = {297},
      year         = {2021},
      abstract     = {The myxoma virus has become of interest in human medicine
                      in the last two decades as it has the ability to infect many
                      types of human cancer cells and is being used as a platform
                      to develop viro-therapeutic agents that suppress aggressive
                      and damaging immune responses and inflammation. Furthermore,
                      the myxoma virus encodes proteins that have strong
                      immunosuppressive effects, and several of the myxoma
                      virus-encoded immunomodulators are being developed to treat
                      systemic inflammatory syndromes such as cardiovascular
                      disease and transplant rejection. Myxoma virus encodes the
                      M-T7 protein, the most abundantly secreted protein expressed
                      in myxoma virus-infected cells, originally identified as a
                      rabbit species-specific interferon-gamma (IFN-γ) receptor
                      homolog and as a chemokine-modulating protein binding a wide
                      range of mammalian chemokines. M-T7 is a critical virulence
                      factor for viral pathogenesis that increases virus lethality
                      when expressed. Although M-T7 has been extensively studied
                      using biochemical and biophysical techniques and its
                      interactome map is well known, its three-dimensional (3D)
                      structure remains elusive. Obtaining the 3D structure of
                      M-T7 would be greatly beneficial and is a crucial step
                      toward advancing M-T7 research through understanding the
                      molecular function and activity of M-T7 as a novel
                      therapeutic reagent and to rationally develop this protein
                      as a drug. This chapter provides an overview of the
                      structural determination techniques, especially X-ray
                      crystallography, that can be applied toward the goal of
                      achieving the first high-resolution structure of M-T7. In
                      addition, details of up-and-coming methods are discussed,
                      including X-ray diffraction at X-ray free electron lasers
                      (XFELs), nuclear magnetic resonance (NMR), cryo-electron
                      microscopy (cryo-EM), Micro-electron diffraction (Micro-ED),
                      and small-angle X-ray scattering (SAXS), and their potential
                      applications to M-T7 structural biology.},
      cin          = {EMBL-User},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)3},
      pubmed       = {pmid:33108661},
      doi          = {10.1007/978-1-0716-1012-1_8},
      url          = {https://bib-pubdb1.desy.de/record/472123},
}