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. Author manuscript; available in PMC: 2024 Apr 6.
Published in final edited form as: Structure. 2023 Mar 16;31(4):480–491.e4. doi: 10.1016/j.str.2023.02.009

Table 1.

Cryo-EM single particle data collection and refinement statistics.

PfCSP in complex with L9 (Class 1) PfCSP in complex with L9 (Class 2)
EMDB ID 28192 28196

PDB ID 8EK1 8EKA

Data Collection
Microscope FEI Glacios FEI Glacios
Voltage (kV) 200 200
Electron dose (e2) 63.7 63.7
Detector Gatan K3 Gatan K3
Pixel Size (Å) 0.46 0.46
Defocus Range (μm) −0.3 to −2.2 −0.3 to −2.2
Magnification 36000 36000
Reconstruction
Software cryoSparcV3.3 cryoSparcV3.3
Particles 117,479 62,735
Symmetry C1 C1
Box size (pix) 320 320
Resolution (Å) (FSC0.143) 3.64 3.72
Refinement
Software Phenix 1.18 Phenix 1.18
Protein residues 1102 905
Chimera CC 0.83 0.84
EMRinger Score 2.83 2.26
R.m.s. deviations
 Bond lengths (Å) 0.004 0.003
 Bond angles (°) 0.735 0.681
Validation
Molprobity score 2.04 2.03
Clash score 9.39 7.54
Favored rotamers (%) 99.47 100
Ramachandran
 Favored regions (%) 90.31 87.40
 Allowed regions (%) 9.23 12.26
 Outlier regions (%) 0.46 0.34