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. Author manuscript; available in PMC: 2022 Dec 1.
Published in final edited form as: Proteins. 2022 Feb 18;90(6):1242–1246. doi: 10.1002/prot.26310

Table 1:

Summary of data collection and refinement statistics.

LmHsp100N

Data collection

Space group P 41 21 2
Unit cell dimensions
a, b, c (Å) 60.971, 60.971, 71.807
 α, β, γ (°) 90.0, 90.0, 90.0
Wavelength (Å) 0.9794
Resolution (Å) 50.00–1.05 (1.07–1.05)
Unique reflections 61,983
Rsym or Rmerge 0.071 (0.528)
R pim 0.023 (0.259)
I / σI 10.9
Completeness (%) 97.1 (92.6)
Redundancy 9.1 (4.8)
Refinement
Resolution (Å) 36.96–1.06
No. reflections 41,615 / 2,515
Rwork / Rfree 0.1339 / 0.1528
No. atoms 1,349
 Protein 1,145
 Ligand/ion 6
 Water 198
B-factors (Å2)
 Protein 19.83
 Ligand/ion 19.35
 Water 30.46
RMS deviation
 Bond lengths (Å) 0.004
 Bond angles (°) 0.721
Ramachandran
 Outliers 0.00%
 Allowed 0.71%
 Favored 99.29%
*

Values in parentheses are for highest-resolution shell.