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Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions.

MPS-Authors

Deckert,  J.
Max Planck Society;

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Hartmuth,  K.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Behzadnia,  N.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Will,  C. L.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Kastner,  B.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Stark,  H.
Research Group of 3D Electron Cryo-Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Luehrmann,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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287669.pdf
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Citation

Deckert, J., Hartmuth, K., Boehringer, D., Behzadnia, N., Will, C. L., Kastner, B., et al. (2006). Protein composition and electron microscopy structure of affinity-purified human spliceosomal B complexes isolated under physiological conditions. Molecular and Cellular Biology, 26(14), 5528-5543. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1592722.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-93E2-9
Abstract
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