Table 1 X-ray diffraction data processing and refinement statistics.

From: Insulin in motion: The A6-A11 disulfide bond allosterically modulates structural transitions required for insulin activity

 

cis isomer

trans isomer

Data collection1

  Space group

I213

P213

  Cell dimensions a, b, c (Å)

79.78, 79.78, 79.78

77.28, 77.28, 77.28

  Resolution (Å)

28.20–2.70 (2.80–2.70)2

30–1.55 (1.60–1.55)2

  R merge

0.066 (1.653)

0.144 (5.03)

  I/σ (I)

16.19 (1.13)

11.72 (0.38)

  CC 1/2

0.999 (0.280)

0.999 (0.107)

  Completeness (%)

98.8 (98.9)

0.999 (1.00)

  Redundancy

6.0 (6.2)

10.8 (10.4)

  Molecules/asymmetric unit

1

2

Refinement

  Resolution (Å)

28.20–2.70

30.0–1.55

  No. reflections

2403

22449

  R work/R free

0.223/0.2823

0.195/0.2153

No. atoms

    Protein

404

827

    Ligand/ion

0

0

    Water

0

97

B-factors

    Protein (Å2)

120.

33.4

    Water

n.a.

46.7

R.m.s. deviations

    Bond lengths (Å)

0.011

0.006

    Bond angles (°)

1.5

0.8

  1. 1Diffraction data are from a single crystal in both instances.
  2. 2Resolution limits were set based on the CC 1/2 correlation statistic being assessed significant at the P = 0.001 level of probability.
  3. 3Free set comprised 5% of the reflections.
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