Table 1 Crystallography data processing and refinement statistics

From: Proteolytic processing induces a conformational switch required for antibacterial toxin delivery

Data processing

Protein

CdiA-CT•CdiIEC3006

Wavelength (Ă…)

0.9793

Resolution range (Ă…)a

30.00 – 2.25 (2.29 – 2.25)

Space group

P212121

Unit cell parameters (Ă…)

41.00, 71.77, 175.54

Unique reflections

25,933 (1274)

Multiplicity

25.4 (17.2)

Completeness (%)

99.9 (99.7)

<I>/<σI>

30.29 (1.77)

Rmergeb

0.132 (1.242)

CC1/2c

0.635

CC*c

0.881

Refinement

Resolution (Ă…)

29.26 – 2.25

Reflections work/test set

23,763/1652

Rwork/ Rfreed

0.182/0.234

Average B factor (Ă…2) (No of atoms)

 

   macromolecule

65.3 (3677)

   solvent

51.2 (109)

Rmsd bond lengths (Ă…)

0.007

Rmsd bond angles (°)

0.786

Ramachandran favorede (%)

96.79

Ramachandran outliers

0.21

Clashscoree

2.6

PDB ID

6VEK

  1. aValues in parentheses correspond to the highest resolution shell.
  2. bRmerge = ΣhΣj | Ihj–<Ih > |/ΣhΣjIhj, where Ihj is the intensity of observation j of reflection h.
  3. cAs defined by ref. 68.
  4. dR = Σh | Fo | –|Fc | /Σh | Fo | for all reflections, where Fo and Fc are observed and calculated structure factors, respectively. Rfree is calculated analogously for the test reflections, randomly selected and excluded from the refinement.
  5. eAs defined by Molprobity69 and implemented in Phenix.
Back to article page