Table 2 X-ray data collection and refinement statistics.

From: “Redirecting an anti-IL-1β antibody to bind a new, unrelated and computationally predicted epitope on hIL-17A”

 

Free AAL160 Fab

AAL160 Fab/IL-1β complex

11.003 Fab /IL-17A complex

Data collection

Space group

P212121

C2

P212121

Cell dimensions

      a, b, c (Å)

62.17, 89.83, 123.73

185.79, 37.17, 97.07Å

83.996, 107.335, 269.297

      α, β, γ (°)

90.000, 90.000, 90.000

90.000, 114.92, 90.000

90.000, 90.000, 90.000

Resolution (Å)

2.00 (2.07–2.00)

3.30 (3.42–3.30)

1.899 (1.931–1.899)*

Rmerge

0.050 (0.381)

0.159 (0.505)

0.130 (2.612)

Rmeas

  

0.138 (2.752)

Rpim

  

0.045 (0.856)

I/σI

11.7

5.3

11.1 (1.1)

CC1/2 (%)

  

0.998 (0.292)

Completeness (%)

99.9 (100.0)

97.7 (86.1)

98.8 (98.0)

Multiplicity

8.4

4.1

10.2 (10.9)

Refinement

Resolution (Å)

16.38–2.00

29.34–3.30

134.65–1.899

No. reflections

47,440

9257

188,538

Rwork/Rfree

0.196/0.217

0.238/0.269

0.2013/0.2273

No. atoms

      Protein

3271

4456

16,443

      Water

317

0

1507

      Buffer components

98 (7x PEG 200)

0

18 (3 glycerol mol.)

B-factors (Å2)

      Fab Lc (chain A, C, E, L)

37.4

65.1

35.5, 41.1, 48.9, 37.8

      Fab Hc (chain B, D, F, H)

35.8

45.6

36.8, 39.3, 42.3, 37.9

      Antigen (chain G, I, J, K)

-

70.9

46.0, 42.8, 48.9, 42.6,

      Water (chain W)

47.2

-

46.6

R.m.s. deviations

      Bond lengths (Å)/angles (°)

0.008/1.01

0.008/1.07

0.008/0.98

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