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Table 1 Data collection, phasing, and refinement statistics for the structure of cMCR-1

From: Structure of the catalytic domain of the colistin resistance enzyme MCR-1

  cMCR-1 (PDB ID 5K4P)
Data collection
 Space group P43212
 Cell dimensions  
   a, b, c, Å 59.1, 59.1, 186.7
   α, β, γ, ° 90, 90, 90
 Wavelength, Å 1.00
 Resolution, Åa 49.9–1.32 (1.39–1.32)
R merge 0.057 (0.491)
R meas 0.079 (0.892)
R pim 0.055 (0.552)
I/s(I) 9.6 (1.7)
CC 1/2 0.996 (0.547)
 Completeness, % 100 (100)
 Redundancy 14.7 (11.7)
Refinement
 Resolution, Å 49.9–1.32 (1.39–1.32)
 No. reflections 78753
R work/R free 0.1464/0.1732
 No. atoms 2935
  Protein 2541
  Ligand/ion (D-sorbitol/zinc) 12/10
  Water 368
B factors, Å2  
  Protein 12.1
  Zinc 10.8
  D-sorbitol 11.3
  Water 25.1
 Root-mean-square deviations  
  Bond lengths, Å 0.007
  Bond angles, ° 0.878
 MolProbity clash score 1.00
  1. aValues in parentheses are for highest resolution shell