Table 1 Crystallographic statistics and refinement details.

From: Structure of GrlR–GrlA complex that prevents GrlA activation of virulence genes

 

SelMet SAD

Data collection

 Space group

C2221

 Cell dimensions

a, b, c (Å)

a=83.19, b=121.21, c=84.83

α, β, γ (°)

90

 Wavelength

0.97893

 Resolution (Å)

50.0–2.62(2.67–2.62)

 aRsym or Rmerge

0.12 (0.39)

 I/σI

16.23 (3.56)

 Completeness (%)

98.0 (82.8)

 Redundancy

13.9 (10.6)

Refinement

 Resolution (Å)

15.0–2.7

 No. of reflections

22,108

 bRwork/cRfree

0.18/0.23

 No. of atoms

Protein

2,543

Ligand/ion

26

Water

15

 B-factors

Protein

53.9

Ligand/ion

54.80

Water

45.7

 r.m.s.d.

Bond lengths (Å)

0.01

Bond angles (°)

1.283

  1. r.m.s.d., root mean squared deviation; SAD, single-wavelength anomalous dispersion.
  2. aRsym=Σ|Ii −<I>|/Σ|Ii| where Ii is the intensity of the ith measurement, and <I> is the mean intensity for that reflection.
  3. bRwork=Σ|Fobs−Fcalc|/Σ|Fobs| where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively.
  4. cRfree=as for Rwork, but for 10.0% of the total reflections chosen at random and omitted from refinement. Individual B-factor refinement was carried out.
  5. *Values in the parenthesis are the highest resolution bin values.
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