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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