2014-12-10 OBS 2013-12-02 RCSB RCSB 2013-12-25 2014-12-10 2014-12-10
Entry withdrawn at author request upon expiration of one-year hold.
Closed conformation of the bacteriophage EL encoded chaperonin Molugu SK, Hildenbrand ZL, Tafoya DA, Herrera N, Enriquez AS, Morgan DG, Sherman MB, He L, Georgopoulos C, Sernova NV, Kurochkina LP, Mesyanzhinov VV, Miroshnikov KA, Bernal RA chaperonin, bacteriophage EL Molugu SK, Hildenbrand ZL, Tafoya DA, Herrera N, Enriquez AS, Morgan DG, Sherman MB, He L, Georgopoulos C, Sernova NV, Kurochkina LP, Mesyanzhinov VV, Miroshnikov KA, Bernal RA Ring separation highlights the protein folding mechanism used by the phage EL encoded chaperonin To Be Published emd_5826.map.gz Image stored as Reals 160 160 160 -79 -79 -79 80 80 80 160 160 160 331.19998 331.19998 331.19998 90.0 90.0 90.0 X Y Z -12.22833729 10.97820187 -0.00071722 0.91209513 1
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2.07 2.07 2.07 2.72 Reconstruction of the closed (ADP) conformation of the phiEL chaperonin
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1 Bacteriophage EL encoded chaperonin in the presence of ADP heptamer protein chaperonin Pseudomonas phage EL true heptamer Escherichia coli BL21 ETHANE FEI VITROBOT MARK III FIELD EMISSION GUN BRIGHT FIELD FLOOD BEAM GATAN ULTRASCAN 4000 (4k x 4k) JEOL 3200FS 01-DEC-2009 GATAN LIQUID NITROGEN 300 60000 200 particle 2.5 singleParticle MRC, EMAN 11.7 FSC 0.5, gold-standard C7 70000