Table 1 Data collection, phasing, and refinement statistics for OPCML (MR-SAD)

From: Inactivating mutations and X-ray crystal structure of the tumor suppressor OPCML reveal cancer-associated functions

 

Native

K2PtCl4

Data collection

Space group

P41212

I4122

Cell dimensions

  

a, b, c (Å)

93.6, 93.6, 262.2

98.8, 98.8, 267.1

α, β, γ (°)

90, 90, 90

90, 90, 90

Resolution (Å)

18.5–2.65 (2.74–2.65)a

48.3–3.17 (3.25–3.17)

R sym

17.1 (273.6)

18.7 (301.5)

R pim

4.7 (73.8)

3.6 (56.6)

I/σ(I)

9.7 (1.2)

11.5 (1.1)

CC 1/2

100 (68.5)

100 (82.3)

Completeness (%)

95.8 (88.8)

100.0 (100.0)

Redundancy

14.4 (14.5)

28.2 (29.1)

Refinement

Resolution (Å)

18.5–2.65 (2.74–2.65)

 

No. reflections

33374 (3021)

 

Rwork/Rfree

28.7/30.4

 

No. atoms

4392

 

Protein

4216

 

Ligand/ion (carbohydrate)

134

 

Water

42

 

B factors

  

Protein

84.6

 

Ligand/ion

91.0

 

Water

74.2

 

R.m.s deviations

  

Bond lengths (Å)

0.006

 

Bond angles (°)

0.99

 

NCS RMSD (Å)

  

All domains

1.10

 

D1 (43–134)

0.24

 

D2 (135–222)

0.19

 

D3 (223–319)

0.64

 
  1. aValues in parentheses are for highest-resolution shell
Back to article page