Table 1 Data collection and refinement statistics

From: Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin

 

Kif2C–tubulin–DARPin

Data collection a

 Space group

C2221

 Cell dimensions

  a, b, c (Å)

51.8, 229.8, 293.9

  α, β, γ (°)

90.0, 90.0, 90.0

 Resolution (Å)

49.0–3.19 (3.38–3.19)

 R meas

0.21 (2.93)

 II

5.34 (0.43)

 CC1/2

0.995 (0.342)

 Multiplicity

3.56 (3.06)

 Completeness (%)

97.3 (85.9)

 Anisotropy directionb

Resolution where CC1/2 > 0.30

  overall (Å)

3.26

  along h axis (Å)

4.83

  along k axis (Å)

3.21

  along I axis (Å)

3.19

 Completeness after anisotropy correction (%)

66.3 (23.4)

Refinement

 Resolution (Å)

42.91–3.19

 No. reflections

19903

 R work/R free

0.211/0.257

 No. atoms

  Protein

10299

  Ligand

122

  Water

0

 B factors

  Protein

104.2

  Ligand

94.6

 Coordinate error (Å)

0.48

 R.m.s.d.

  Bond lengths (Å)

0.010

  Bond angles (°)

1.10

 Ramachandran

  Favored region (%)

96.11

  Allowed region (%)

3.05

  Outliers (%)

0.84

  1. aData were collected on a single crystal. Values in parentheses are for the highest-resolution shell
  2. bThe anisotropy statistics were computed with AIMLESS39