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Figure 5
Comparing side chains of PASR-processed apoferritin data achieving <2 Å resolution and directly comparing with EMD-9599 at 1.63 Å resolution. When reprocessing EMPIAR-10216, 1.71 Å resolution was achieved while PASR achieved 1.78 Å resolution. Six example side chains of varying quality are shown; In EMD-9599, the five-member-ring nature of His128 is clear, while with PASR the hole is less well defined. Lys146 and Phe132 are comparable. Trp93 shows clear holes for both the five- and six-member rings for both the original data and PASR. For both the original data and PASR processing, the density of tyrosine is dependent on location; Tyr34 is weaker, while Tyr168 is clear and strong with a clear hole in the six-membered ring. Density maps are displayed at 5σ. Even at <2 Å resolution, PASR is competitive in terms of clarity with data collected at the higher magnification in counting mode.

IUCrJ
Volume 13| Part 5| September 2026| Pages 589-605
ISSN: 2052-2525
https://doi.org/10.1107/S2052252526005348