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. 2024 Mar 29;7:380. doi: 10.1038/s42003-024-06078-9

Table 3.

Data collection and refinement statistics (Molecular Replacement)

MmaSAHH•NAD•inosine PfuSAHH•NAD•inosine PfuSAHH•NAD•inosine (95 °C) PfuSAHH•NAD•SIH SacSAHH•NAD•adenosine MmSAHH•NAD•inosine
Data collection
Space group P21 P42212 P42212 P42212 P1 I222
Cell dimensions
   a, b, c (Å) 65.8, 328.9, 85.1 112.5, 112.5, 122.8 111.7, 111.7, 122.1 111.7, 111.7, 121.6 84.4, 88.4, 138.6 98.2, 102.5, 173.4
   α, β, γ (°) 90, 107.2, 90 90, 90, 90 90, 90, 90 90, 90, 90 78.9, 74.9, 64.9 90, 90, 90
Resolution [Å]

45.44–2.65

(2.74–2.65)

48.62–2.28

(2.37–2.28)

48.31–2.03

(2.11–2.03)

53.4–2.05

(2.12–2.05)

46.16–2.50

(2.59–2.50)

54.9–2.48

(2.56–2.48)

Rmerge

0.1748

(1.075)

0.1495

(1.191)

0.2373

(2.425)

0.1048

(0.9204)

0.1348

(0.582)

0.177

(0.97)

II

6.73

(2.13)

13.51

(1.66)

15.36

(1.54)

16.82 (2.70)

6.67

(2.35)

7.8

(2.1)

Completeness [%]

97.3

(98.2)

99.8

(98.8)

99.7

(97.6)

99.7

(99.9)

87.5

(85.9)

98.8

(99)

Redundancy

3.6

(3.5)

12.7

(8.3)

26.8

(26.6)

12.8

(13.4)

3.6

(3.6)

5.7

(5.9)

Refinement
Resolution [Å]

45.44–2.65

(2.74–2.65)

48.62–2.28

(2.37–2.28)

48.31–2.03

(2.11–2.03)

53.4–2.05

(2.12–2.05)

46.16–2.50

(2.59–2.50)

54.9–2.48

(2.56–2.48)

No. reflections

141280

(13525)

36333

(3519)

50113

(4818)

48676

(4780)

105739

(10341)

31048

(3056)

Rwork /Rfree [%] 18.8/24.3 16.1/21.6 15.5/20.3 17.6/21.9 22.9/28.2 17.0/21.8
No. atoms 26322 6891 7086 7147 27556 7067
   Protein 25440 6604 6660 6706 25760 6650
   Ligand/ion 608 126 126 88 504 128
   Water 274 161 300 353 1292 289
B-factors 67.14 46.77 35.81 38.41 40.96 40.98
   Protein 67.59 46.98 35.67 38.16 40.23 41.16
   Ligand/ion 55.84 38.49 28.84 34.81 31.83 35.81
   Water 50.24 44.84 41.95 44.11 59.02 39.23
R.m.s. deviations
   Bond lengths (Å) 0.030 0.014 0.009 0.014 0.008 0.014
   Bond angles (°) 2.33 1.81 1.48 1.84 1.69 1.86

Each structure was solved from a single crystal. Values in parentheses are for highest-resolution shell.