Table 2 Data collection and refinement statistics.

From: Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity

Data collection

 

Space group

C2

Cell dimensions

 a, b, c (Å)

250.378, 147.678, 143.972

 α, β, γ (°)

90.000, 103.852, 90.000

Resolution range (Å)

50.00–2.85 (2.90–2.85)

Rmerge (%)a

15.0 (106.8)

CC1/2b

(0.744)

I/σ(I)

14.0 (1.5)

Completeness (%)

99.7 (99.9)

Redundancy

8.2 (8.6)

Refinement

Resolution (Å)

50–2.85 (2.92–2.85)

No. of reflections

117,634 (7732)

Rwork/Rfree (%)c

19.2 (27.0)/23.0 (31.0)

No. of atoms

 Protein

24,569

 Ligand

103

 Water

161

Mean B (Å2)

 Protein

82.0

 Ligand

94.7

 Water

48.8

R.m.s deviations

 Bond lengths (Å)

0.007

 Bond angles (°)

0.922

Ramachandran analysis

 Favored region (%)

97.01

 Allowed region (%)

2.73

 Outliers (%)

0.26

  1. The numbers in parentheses represent values for the highest resolution shell
  2. aRmerge = ∑|Ii − Im|/∑Ii, where Ii is the intensity of the measured reflection and Im is the mean intensity of all symmetry related reflections
  3. bCC1/2 is the correlation coefficient of the half datasets
  4. cRwork = Σ||Fobs| − |Fcalc||/Σ|Fobs|, where Fobs and Fcalc are observed and calculated structure factors
  5. Rfree = ΣT||Fobs| − |Fcalc||/ΣT|Fobs|, where T is a test data set of about 1.7 % of the total reflections randomly chosen and set aside prior to refinement
Back to article page