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Table 1 Data collection, phasing, and refinement statistics of AcrIE2

From: Biochemical characterization of type I-E anti-CRISPR proteins, AcrIE2 and AcrIE4

 

Native

Selenomethionyl

Space group

P212121

P212121

Unit cell parameters (Å)

a = 26.96, b = 47.35, c = 56.37

α = β = γ = 90°

a = 26.95, b = 47.45, c = 56.44

α = β = γ = 90°

Wavelength (Å)

0.9792

0.9792

Data collection statistics

 Resolution range (Å)

50.00–1.23 (1.27–1.23)a

50.00–1.44 (1.49–1.44)a

 Number of reflections

21,354 (2072)a

13,392 (1310)a

 Completeness (%)

98.3 (97.8)a

98.4 (97.3)a

 Rmergeb

0.092 (0.290)a

0.123 (2.451)a

 CC1/2

0.990 (0.974)a

0.997 (0.583)a

 CC*

0.997 (0.993)a

0.999 (0.858)a

 Redundancy

13.8 (13.2)a

13.3 (12.2)a

 Mean I/σ

25.59 (8.84)a

11.46 (1.56)a

Phasing statistics

 f′, f″ used in phasing

 

− 7.54, 3.36

 Figure of merit

 

0.384

Refinement statistics

 Resolution range (Å)

28.2–1.23

 

 Rcrystc/Rfreed (%)

18.1/19.9

 

 RMSD bonds (Å)

0.006

 

 RMSD angles (deg)

1.003

 

 Average B-factor (Å2)

13.1

 

 Number of water molecules

118

 

 Ramachandran favored (%)

100

 

 Ramachandran allowed (%)

0

 
  1. aValues in parentheses are for the highest-resolution shell
  2. b\({\text{R}}_{{{\text{merge}}}} ~ = \Sigma _{{\text{h}}} \Sigma \left| {{\text{I}}_{{\text{i}}} \left( {\text{h}} \right) - < {\text{I}}\left( {\text{h}} \right) > } \right|/\Sigma _{{\text{h}}} \Sigma _{{\text{i}}} {\text{I}}_{{\text{i}}} \left( {\text{h}} \right),\) where Ii(h) is the intensity of an individual measurement of the reflection and < I(h) > is the mean intensity of the reflection.
  3. c\({\text{R}}_{{{\text{cryst}}}} = \Sigma _{{\text{h}}} \left| {\left| {{\text{F}}_{{{\text{obs}}}} } \right| - \left| {{\text{F}}_{{{\text{calc}}}} } \right|} \right|/\Sigma _{{\text{h}}} \left| {{\text{F}}_{{{\text{obs}}}} } \right|,\) where Fobs and Fcalc are the observed and calculated structure factor amplitudes, respectively
  4. dRfree was calculated as Rcryst using ~ 5% of the randomly selected unique reflections that were omitted from structure refinement