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Table 2 Data collection, phasing, and structure refinement statistics of SsTRIC

From: Ion- and water-binding sites inside an occluded hourglass pore of a trimeric intracellular cation (TRIC) channel

Data collection CH3HgCl (A15C mutant) KCl (wild type) TlNO3 (anomalous)
Wavelength (Å) 1.00000 1.00137 1.5418
Beamlinea SSRF BL17U SSRF BL17U Rigaku MicroMax-007
Space group C 2 C 2 C 2
Resolution (Å) 50–2.5 (2.64–2.5) 50–2.2 (2.32–2.2) 50–3.4 (3.52–3.4)
Cell dimensions (Å, °) a = 152.07 a = 152.07 a = 150.40
b = 87.48 b = 87.73 b = 86.44
c = 173.62 c = 173.06 c = 173.30
β = 108.75 β = 108.90 β = 108.59
R sym 0.211 (0.883) 0.149 (0.604) 0.133 (0.886)
R pim b 0.076 (0.308) 0.075 (0.300) N/A
I/σ 8.1 (3.9) 7.1 (2.7) 12.1 (2.1)
Completeness (%) 98.8 (96.9) 97.6 (94.8) 88.6 (87.2)
Redundancy 8.9 (8.7) 4.7 (4.6) 5.9 (6.0)
Phasing statistics
 No. of heavy atom sites 6   
 Figure of merit (before/after DM) 0.258 (0.640)  
Refinement statistics
 Resolution   50–2.2  
 No. of reflections (no. of reflections in free set)   106,561 (2614)
R work (%)   21.08
R free (%)   22.85
No. atoms (B-factors, Å2)
 All atoms   9642 (38.1)  
 Protein   9054 (37.0) (6 chains)
 Cation   33 K+ (77.9)
 Water   381 (46.0)
 Others (detergent)   174 (68.4)
 Ramachandran plot (%)c   96.8/2.5/0.7
 RMSD bond length (Å)   0.007
 RMSD bond angles (°)   1.22
  1. The R sym , R pim , I/σ, completeness, and redundancy are presented as the statistics for overall and outmost shell (in parentheses)
  2. a SSRF Shanghai Synchrotron Radiation Facility
  3. b R pim is the precision-indicating (multiplicity-weighted) R sym reported by the Scala program. R pim  = ∑ hkl [1/(N − 1)]1/2 i |I i (hkl) − 〈I(hkl)〉|/∑ hkl i I i (hkl) The HKL2000 program used to process TlNO3 data did not report R pim statistics
  4. cPercentage of residues in most favored, additional allowed, and generously allowed regions in Ramachandran plot. No residues are observed in the disallowed region