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Table 1 Data collection and refinement statistics of the dysferlin inner DysF domain

From: Crystal structures of the human Dysferlin inner DysF domain

Data collection

PDB 4CAI

PDB 4CAH

Wavelength (Ã…)

1.037530

0.97718

Space group

P212121

P213

Unit-cell parameters

  

  a, b, c (Å)

74.5, 77.47, 79.89

75.95, 75.95, 75.95

  α, β, γ (o)

90, 90, 90

90, 90, 90

Resolution range (Ã…)

50-2.2 (2.27-2.20)

53.7-1.9 (1.94-1.9)

Total number of observation

78153 (6922)

115092 (7574)

Total number unique

24062 (2084)

11803 (760)

Completeness

99.8 (99.9)

100.0 (100.0)

Multiplicity

3.2 (3.3)

9.8 (10)

<I/σ(I)>

12.4 (2.3)

30.5 (3.5)

CC(1/2)

0.976 (0.758)

1.00 (0.847)

Rmerge

0.045 (0.466)

0.044 (0.667)

Solvent content (%)

56.8

53.0

Molecule per ASU

3

1

Wilson B factor (Ã…2)

42.2

31.05

Refinement

  

Resolution range (Ã…)

44.57-2.2

53.7-1.9

Rwork

0.1858 (0.2457)

0.1775 (0.1932)

Rfree

0.2271 (0.3102)

0.1908 (0.2283)

Reflection, working

22764

11220

Reflection, free

1206

549

Average B factor

61.0

42.0

Rmsd bond angle

1.358

1.76

Rmsd bond length (Ã…)

0.011

0.015

Ramachandran Analysis

  

Preferred region (%)

96.7

95.2

Allowed region (%)

2.4

2.9

Outliers (%)

0.9

1.9

  1. Values in parentheses refer to the highest resolution shell.
  2. Rmerge = Σ (I - < I>) / Σ < I > .
  3. Rwork = Σ (|Fobs |- |Fcalc|)/ Σ|Fobs| for 95% of data. Rfree is the same equation for 5% of the data excluded from refinement.