Table 3 Data collection and refinement statistics

From: Structural insights into trans-histone regulation of H3K4 methylation by unique histone H4 binding of MLL3/4

 

MLL3_ePHD6–H4 peptide

Data collection

 Space group

P6

 Cell dimensions

   a, b, c (Å)

85.9, 85.9, 98.7

  α, β, γ (°)

90, 90, 120

 Resolution (Å)

43.00–1.80(1.83–1.80)a

 Rsym or Rmerge

9.8(135.7)

 I / σI

18.7(1.5)

 Completeness (%)

100.0(99.5)

 Redundancy

10.0(9.2)

Refinement

 Resolution (Å)

43.00–1.80

 No. reflections

36,874(1507)

 Rwork/Rfree

19.4/21.6

 No. atoms

  Protein

2766

  Ligand/ion

99/14

  Water

143

 B-factors

  Protein

30.1

  Ligand/ion

40.9/23.5

  Water

33.4

 R.m.s. deviations

  Bond lengths (Å)

0.010

  Bond angles (°)

1.4

  1. aValues in parentheses are for highest-resolution shell
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