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Table 1 Grb7 SH2 domain Data Collection and Refinement Statistics

From: Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation

Grb7 SH2

 

Data Collection

 

Space group

P2 1 2 1 2 1

Unit Cell (Ã…)

a = 62.6

 

b = 63.9

 

c = 105.7

 

α = β = γ = 90°

Molecules in the ASU

4

Resolution range (Ã…)a

44 – 2.1 (2.18 – 2.1)

Observations

79384

Unique reflections

25401

Completeness (%)a

99.1 (99.4)

I/σa

12.6 (2.2)

Rmerge (%)a, b

8.4 (50.5)

Wilson B (Ã…)a

28.4

Refinement

 

Resolution limits (Ã…)a

30 – 2.10 (2.15 – 2.10)

No. of reflectionsa

23949 (1731)

Rcryst (%)a

20.1 (25.4)

Rfree (%)a, c

25.5 (28.9)

Protein atoms

3733

Water molecules

181

Other molecules

7 SO42-

r.m.s.d. from ideal values ideaiations

 

Bond lengths (Ã…)

0.014

Bond angles (°)

1.486

Average B-factors (Ã…)3

 

Protein

38.1

Water

40.6

Ions

58.7

  1. aValues in parentheses are for the highest resolution shell happiness
  2. bRmerge = Σ |I – < I >|/Σ I where I is the observed diffraction intensity of the jth observation of reflection hkl and < I > is the average diffraction intensity of all measurements of reflection hkl.
  3. cRfree = Σ | |Fo|-|Fc|/Σ |Fo| where |Fo| and |Fc| are the observed and calculated factors respectively.