Table 1 Data collection and structure refinement statistics of DUX4 HD2 associated with ERG site

From: DUX4HD2-DNAERG structure reveals new insight into DUX4-Responsive-Element

Protein

DUX4HD2-DNAERG

Data collection

Space group

P31

Unit cell dimension (Ã…)

  a

32.6

  b

32.6

  c

126.6

Molecule per ASU

2HD2, 1 double-chain DNAERG

Derivative

Native

Source/Stationa

BL19U

Wavelength (Ã…)

0.9785

Resolution range (Ã…)

63.3–1.60

Observations (I / σ(I) > 0)

160629

Unique reflections (I / σ(I) > 0)

19696 (2803)

High-resolution shell (Ã…)

1.69–1.60

Rsym (%)b,c:

7.2 (91.2)

<I / σ(I)>c:

11.4 (1.8)

Completenessc (%):

99.2 (97.0)

Redundancyc:

8.2 (6.8)

CC1/2

0.99 (0.76)

Structure refinement

 Resolution range (Å)

28.2–1.60

 R-factor (%)

20.1

 R-factor (high-resolution shell)d

28.3

 Rfree (%)e

20.7

 Rfree (high-resolution shell)

34.7

 Total number of non-hydrogen atoms

1492

   Protein atoms

1376

   Water molecules

116

R.m.s. deviations:f

  Bond length (Å)

0.013

  Bond angle (°)

1.227

  Main chain B-factors (Å2)

3.676

  Side-chain B-factors (Å2)

7.047

Wilson B-factor (Ã…2)

28.4

Average B-factor protein atoms (Ã…2)

40.3

Ramachandran statistics (%)

  Most favored region

96.4

  Allowed regions

3.6

  Outliers

0

  1. aBeamline designations refer to the Shanghai Synchrotron Radiation Facility, Shanghai, P. R. of China
  2. bRsym = Σ(I- < I > )2/ΣI2
  3. cOverall, high-resolution shell in parentheses
  4. dHigh-resolution shell: 1.6847–1.6000
  5. eRfree calculated using 5% of total reflections omitted from refinement
  6. fR.m.s. deviations report root mean square deviations from ideal bond lengths/angles and of B-factors between bonded atoms [8]