Table 1 Crystallographic data for BoGT6a and BoGT6a-2′-fucosyllactose (FAL) complex

From: Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen

 

BoGT6a

BoGT6a-FAL

Space group

P4322

P21

Number of molecules per asymmetric unit

1

4

Cell dimensions

a = 41.23 Å, b = 41.23 Å, c = 282.9 Å

a = 70.85 Å, b = 93.87 Å, c = 75.51 Å

 

α = β = γ = 90°

β = 93.8°

Resolution range (Å)

33.32–1.91†

70.69–3.00

Rsymma (outer shell)

0.075 (0.14)††

0.13 (0.49)

I/σI (outer shell)

18.1 (4.5)

9.3 (2.6)

Completeness (outer shell) %

77.9 (22.2)

94.1 (93.7)

Total no. of reflections

600206

72365

Unique no. of reflections

20120

18641

Redundancy (outer shell)

4.3 (1.6)

3.9 (3.8)

Wilson B-factor (Å2)

20.0

47.78

Rcrystb/Rfreec

17.91/23.19

18.07/26.19

Average B-factor (Å2)

  

Overall

14.0

36.6

Protein

10.9

A: 30.5, B: 35.2, C: 41.7, D: 38.8

Ligand

27.1 (HEPES); Cl− (10.8); Ca2+ (13.3)

36.2 (FAL)

Water

19.1

—

RMSD values

  

bond length (Å)

0.008

0.009

bond angle (°)

1.114

1.429

Ramachandran plot statistics (%)

  

Favoured

98.6

96.7

Additionally allowed

1.4

3.3

PDB code

4AYL

4AYJ

  1. aRsymm = ΣhΣi|I(h) − i(h)|/ΣhΣiIi(h), where Ii(h) and I(h) are the ith and the mean measurements of the intensity of reflection h, respectively.
  2. bRcryst = Σh|Fo − Fc|/ΣhFo, where Fo and Fc are the observed and calculated structure factor amplitudes of reflection h, respectively.
  3. cRfree is equal to Rcryst for a randomly selected 5.0% subset of reflections not used in the refinement.
  4. †Reflections up to 1.91 Å resolution were used in all crystallographic calculations.
  5. ††Due to low Rsymm value, resolution cutoff of 1.91 Å was used and the crystal diffracted up to 1.7 Å. Data completeness figures at 2.1 Å are – overall and last shell (2.18–2.1 Å) are 90.5 and 67.6% respectively.
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