Table 1 Data collection and refinement statistics.

From: Structure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitors

 

IRE1α MKC9989

IRE1α OICR573

IRE1α OICR464

Data collection

 Space group

C 1 2 1

C 1 2 1

C 1 2 1

 Cell dimensions

a, b, c (Å)

246.08, 90.5, 72.13

319.24, 63.03, 140.78

319.11, 62.31, 141.33

α, β, γ (°)

90.00, 91.88, 90.00

90.00, 99.49, 90.00

90.00, 99.57, 90.00

 Resolution (Å)

72.09–2.90 (2.98–2.90)

48.27–3.40 (3.60–3.40)

46.60–3.00 (3.18–3.00)

 Rmeas (%)

15.3 (99.8)

17.2 (93.9)

7.8 (91.2)

 Rmerge (%)

35.6 (172.7)

30.9 (121.9)

22.3 (158.0)

 I/σI

7.14 (1.17)

8.69 (1.74)

11.08 (1.33)

 Completeness (%)

96.2 (99.7)

94.5 (97.3)

96.2 (96.6)

 Redundancy

3.69 (3.34)

3.71 (3.71)

2.25 (2.24)

Refinement

 Resolution (Å)

72.09–2.90

48.27–3.40

46.60–3.00

 No. of reflections

21,855

29,201

40,131

 Rwork/Rfree

0.2015/0.2324

0.2219/0.2852

0.2100/0.2759

 No. of atoms

Protein

6,220

12,448

12,316

Ligand/ion

102

165

152

Water

0

0

0

 B factors

Protein

60.0

87.9

90.0

Inhibitor

64.6

115.9

107.7

Other ligands

48.5

71.5

69.3

 r.m.s. deviations

Bond lengths (Å)

0.018

0.006

0.012

Bond angles (°)

1.37

1.18

1.32

  1. Data were collected from a single crystal in each case. Highest-resolution shell is shown in parenthesis.
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