2015-01-14 OBS 2013-09-05 PDBe PDBe 2013-10-09 2015-01-14
hold period expired.
Electron microscopy of the complex formed by chaperones TBCE and TBCB and alpha-tubulin Serna M, Carranza G, Martin-Benito J, Janowsk R, Canals A, Coll M, Zabala JC, Valpuesta JM chaperones, protein folding, protein degradation, tubulin proteostasis Serna M, Carranza G, Martin-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM The structure of the complex formed by chaperones TBCE and TBCB and alpha-tubulin reveals a mechanically driven dissociation of the tubulin dimer To Be Published emd_2449.map.gz Image stored as Reals 24 24 24 0 0 0 23 23 23 24 24 24 111.84 111.84 111.84 90.0 90.0 90.0 X Y Z -0.06966436 0.16886918 0.00422765 0.02536990 1
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4.66 4.66 4.66 0.051 Reconstruction of the human and wildtype TBCE 1 Human Tubulin Binding Cofactor E Monomer 0.059 protein Tubulin binding cofactor E Tubulin-specific chaperone E 0.059 Homo sapiens true Monomer Human 1 Q15813 Cytoplasm pFastBac-1 Spodoptera frugiperda Sf9 NONE NONE Objective lens astigmatism was corrected at 100,000 times magnification TUNGSTEN HAIRPIN 10 BRIGHT FIELD 1000 1500 FLOOD BEAM KODAK SO-163 FILM 5.6 JEOL 1200EXII 01-FEB-2011 JEOL 100 60000 ZEISS SCAI 68 14 Grids with adsorbed protein floated on 2% w/v uranyl acetate for 1 min. particle 0.01 300 mesh copper grid with thin carbon support, glow discharged in air atmosphere
100mM MES-NaOH, 25mM KCl, 1mM MgCl2, 1mM EGTA
6.7 singleParticle Iterative angular refinement, projection matching EMAN, Spider, XMIPP N. Grigorieff CTFFIND3
Individual particles were manually selected using XMIPP software package.
17 FSC 0.333 C1 12000
The particles were manually selected using the XMIPP program