Table 1 Crystallographic data collection and refinement statistics

From: Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1

 

ΔIBB-importin α3:RCC1

IBB-Kap60: yRCC1

Data collection

 Space group

P1

P212121

Cell dimensions

 a, b, c (Å)

127.4, 162.5, 161.6

91.1, 99.2, 125.0

 α, β, γ (°)

75.7, 85.6, 72.2

90.0, 90.0, 90.0

 Wavelength (Å)

0.97

1.18

 Resolution (Å)

50–3.45 (3.53–3.45)

50–2.63 (2.72–2.63)

 No. of reflections (tot/unique)

935,054/143,482

160,524/33,934

 R sym

13.1 (65.5)

4.9 (64.4)

 R pim

11.2 (65.9)

2.2 (42.8)

 I/σI

12.2 (1.8)

49.9 (3.4)

 Completeness (%)

90.4 (71.5)

96.0 (85.8)

 Redundancy

2.0 (1.6)

4.7 (2.7)

Refinement

 PDB ID

5TBK

5T94

 Resolution (Å)

20–3.45

15–2.63

 No. of reflections

118,199

31,489

 R work/R free*

27.8/29.6

21.7/25.9

 No. of complexes in AU

8

1

 No. of protein atoms

50,677

6808

Ramachandran

 Favored/allowed/outliers

96.1/3.9/0.0

95.3/4.6/0.1

 MolProbity Clashscore

8.8

11.6

R.m.s deviations

 Bond lengths (Å)

0.005

0.002

 Bond angles (°)

0.684

0.496

  1. Values in parentheses are for highest-resolution shells
  2. *R free was calculated using ~5% randomly selected reflections