PMC

Ribosomal protein composition of the 12S RNP particle (A) and of the original 30S subunits (B). Proteins were extracted as described () and analyzed by two-dimensional gel electrophoresis as described () with minor modifications. Nomenclature of ribosomal proteins is according to ref. .

a, Two views of the nucleolar pre-60S particle state 2 model, with Diamond–Blackfan anaemia-associated ribosomal proteins shown in surface representation. b, Rpl15 is located between the 5.8S-domain I duplex and a domain I–domain II interface. c, Rpl33 (Rpl35 in Homo sapiens) binds at the junction of domains I, II and VI in the 25S rRNA. d, Rpl26 associates with the domain I–5.8S rRNA interface and additionally inserts its N terminus (N) between domain I and domain II.

(A) Ribosomal particles were auto-picked from representative -pixel micrographs collected at 1.62 Å/pixel using four template classes, showing near-identical picking with and without low-pass filtering to 20 Å. The only differing particle is indicated in orange, and likely does not depict a ribosomal particle. (B–C) Despite near-identical particle selection, performance is dramatically improved. (D) Filtering alone provides almost 20-fold performance improvement on any hardware compared to previsos versions of relion, and when combined with GPU-accelerated particle picking the resulting performance gain is more than two orders of magnitude using only a single GPU (GTX 1080).
DOI: http://dx.doi.org/10.7554/eLife.18722.009

Tat affects ribosomal profiles from Drosophila female extracts. Ribosomal profiles of control (WG) and transgenic (Tat-strain) strains, subjected (A) and not (B) to heat shock treatment (equal amount of O.D.260 were loaded). Histograms show quantification of 80S particle, (** p < 0.01).