Table 1 Data collection and refinement statistics

From: Structure of Slitrk2–PTPδ complex reveals mechanisms for splicing-dependent trans-synaptic adhesion

Slitrk2 LRR1–PTPδ Ig1-Fn1

Data collection

Wavelength (Å)

1.0000

Resolution (Å)a

50.0–3.35 (3.41–3.35)

Space group

P212121

Cell dimensions

 

 a, b, c (Å)

87.2, 91.3, 123.4

 α, β, γ (°)

90, 90, 90

No. of unique reflections

14,509

Completeness (%)a

99.2 (97.2)

Rsym (%)a,b

13.0 (40.7)

I/σΙa

14.3 (1.9)

Redundancya

9.5 (5.9)

Refinement

 

No. of atoms

 

 Protein

4891

 NAG

56

Rwork/Rfree (%)c

23.46/28.65

R.m.s.d.

 

 Bond lengths (Å)

0.005

 Bond angles (°)

1.113

Average B-factor

 

 Protein

109.6

 NAG

111.2

Ramachandran plot

 

 Most favored (%)

83.6

 Disallowed (%)

0.0

  1. aValues in parentheses are for the highest-resolution shell.
  2. bRsym = ΣhklΣi |Ii(hkl) - <I(hkl)>|/ΣhklΣi Ii(hkl), where Ii(hkl) is the i-th intensity measurement of reflection hkl, including symmetry-related reflections and <I(hkl)> is the average.
  3. cRwork = ∑hkl|FobsFcalc|/∑hkl|Fobs| for work set and Rfree = ∑hkl|FobsFcalc|/∑hkl|Fobs| for test set, which comprises randomly-selected 5% of the total reflections.