Table 1 Data collection and refinement statistics

From: Molecular basis for governing the morphology of type-I collagen fibrils by Osteomodulin

 

Osteomodulin

Data collection

 

 Space group

P 1 21 1

 Cell dimensions

  a, b, c (Å)

75.6, 110.7, 122.2

  α, β, γ (°)

90, 107, 90

 Resolution (Å)

35.2–2.17 (2.28–2.17)

 Rmerge

0.084 (0.644)

 I/σ (I)

9.2 (1.9)

 Redundancy

3.6 (3.1)

 Completeness (%)

99.2 (97.9)

Refinement statistics

 Resolution (Å)

35.2–2.17 (2.28–2.17)

 No. of reflections

 Rwork/Rfree (%)

21.7/24.5

 No. of protein chains

4

 No. of atoms

  Protein

10,014

  Carbohydrate

182

  Other

10

  Water

315

 B-factor (Å2)

  Protein

45.5

  Carbohydrate

79.1

  Others

63.5

  Water

38.8

 RMSD bond (Å)

0.015

 RMSD angle (°)

1.73

  1. The structure was determined from one crystal (the best diffracting crystal)
  2. Values in parentheses are for the highest resolution shell