Table 3 Data collection and refinement statistics.

From: Structural basis of methotrexate and pemetrexed action on serine hydroxymethyltransferases revealed using plant models

 

AtSHMT2-MTX

AtSHMT4-MTX

AtSHMT2-PTX

Data collection

Beamline

APS 22-BM

APS 22-ID

APS 22-BM

Wavelength (Å)

1.0000

1.0000

1.0000

Space group

P212121

P212121

P212121

Unit cell parameters

    a, b, c (Å)

115.4, 130.7, 151.3

118.8, 120.9, 131.8

115.4, 130.8, 151.2

Resolution (Å)

80.0–1.63 (1.73–1.63)

80.0–2.12 (2.25–2.12)

80.0–1.54 (1.64–1.54)

Unique reflections

279297 (44247)

106878 (17038)

330027 (52224)

Multiplicity

8.2 (7.8)

4.2 (4.3)

8.1 (7.7)

Completeness (%)

99.8 (98.5)

98.8 (98.7)

99.7 (98.2)

Rmeas a(%)

9.3 (124.1)

10.8 (76.0)

8.8 (133.8)

<I/σ(I)>

18.3 (2.0)

11.6 (1.9)

18.88 (1.8)

Refinement

Rfree reflections

1396

1068

1320

No. of atoms (non-H)

17397

15779

17445

  protein

15078

14583

15198

  ligands

397

231

311

  solvent

1922

965

1936

Rwork/Rfree (%)

12.5/17.7

17.4/23.4

12.9/16.6

Average B-factor (Å2)

    protein

24.8

38.6

23.8

    ligands

47.7

57.8

45.6

    solvent

41.3

39.3

40.5

rmsd from ideal geometry

    bond lengths (Å)

0.005

0.006

0.005

    bond angles (°)

0.81

0.90

0.79

Ramachandran statistics (%)

    favored

97.9

96.7

97.6

    allowed

2.1

3.4

2.4

    outliers

0.0

0.0

0.0

    PDB ID

6smn

6smr

6smw

  1. Values in parentheses correspond to the highest resolution shell.
  2. aRmeas = redundancy independent R-factor.
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