Table 2 Data collection and refinement statistics for NCP assembled with H2A and either the same blunt-end 145 bp DNA fragment (NCP145) used for the H2A.X structure or the same sticky-end 147 bp DNA fragment (NCP147s) used for the γH2A.X structure.

From: PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome

 

NCP145

NCP147s

Data collection

 Space group

P212121

P212121

 Cell dimensions

      a, b, c (Å)

107.6, 109.7, 183.5

105.3, 109.7, 183.8

      α, β, γ (°)

90, 90, 90

90, 90, 90

 Resolution (Å)

1.99–76.8 (1.99–2.10)a

2.25–94.2 (2.25–2.37)a

 Rmerge (%)

6.8 (212)

9.5 (194)

 Rpim (%)

2.1 (65.2)

3.0 (76.0)

 I/σI

17.4 (1.3)

12.2 (1.0)

 CC½ (%)

99.7 (52.6)

99.7 (61.6)

 Completeness (%)

99.6 (97.9)

99.7 (97.7)

 Redundancy

12.2 (11.6)

11.5 (7.9)

Refinement

 Resolution (Å)

1.99–76.8

2.25–94.2

 No. of reflections

145,312

99,086

 Rwork/Rfree (%)

23.6/26.3

23.9/29.2

 No. of atoms

12,178

12,227

      Protein

6,118

6,129

      DNA

5,939

6,029

      Solvent

121

69

 B-factors (Å2)

79

85

      Protein

53

63

      DNA

106

108

      Solvent

44

66

 R.m.s. deviations

      Bond lengths (Å)

0.008

0.007

      Bond angles (°)

1.474

1.496

  1. aSingle crystal data sets; values within parentheses are for the highest resolution shell