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Table 1 Data collection and refinement statistics

From: Structural characterization of S100A15 reveals a novel zinc coordination site among S100 proteins and altered surface chemistry with functional implications for receptor binding

A. Data collection

S100A15

S100A7D24G

Spacegroup

I2

P43212

a, b, c (Ã…)

52.03, 33.47, 64.05

51.48, 51.48, 117.23

α, β, γ (deg.)

90, 90.81, 90

90, 90, 90

Wavelength

0.9794

0.9794

Resolution range (Ã…)

40.66-1.70 (1.79-1.70)

38.68-1.60 (1.69-1.60)

Measured reflections

44302

203068

Unique reflections

12285

21100

Redundancy

3.6 (3.6)

9.6 (9.8)

Completeness (%)

99.6 (100.0)

99.6 (98.4)

I/σ(I)

8.7 (2.5)

15.3 (2.6)

Rmergea

0.071 (0.385)

0.048 (0.430)

B. Refinement

  

Resolution (Ã…)

28.15-1.70 (1.74-1.70)

34.76-1.60 (1.64-1.60)

Rcrystb

0.199 (0.313)

0.190 (0.250)

Rfreec

0.230 (0.328)

0.225 (0.274)

No. of atoms

  

 Protein

767

773

 Solvent

110

148

 Calcium

1

1

 Zinc

2

1

 Chloride

1

1

B-values (Ã…2)

  

 Protein

30.29

23.42

 Solvent

45.84

41.57

 Calcium

23.60

19.85

 Zinc

30.52

20.80

 Chloride

35.94

24.99

r.m.s.d

  

 Bond lengths (Å)

0.013

0.016

 Bond angles (deg.)

1.321

1.533

Ramachandran statistics

  

Most favoured

97.87

98.91

Allowed

2.13

1.09

Disallowed

0

0