Table 2 Data collection and refinement statistics for the fucosylated IgG1-Fc/sFcγRIIIa complexes.

From: Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa

 

Fucosylated IgG1-Fc/sFcγRIIIa

Fucosylated IgG1-Fc- Y296W/sFcγRIIIa

Crystallographic data

Space group

P41212

P41212

Unit cell a/b/c (Å)

77.6/77.6/351.9

77.3/77.3/349.8

Data processing statistics

Beam line

SPring-8 BL44XU

PF BL5A

Wavelength (Å)

0.90000

1.00000

Resolution (Å)

46.78–2.40 (2.54–2.40)

46.55–2.50 (2.65–2.50)

Total/unique reflections

487,882/43,217

512,558/37,895

Completeness (%)

99.5 (97.1)

99.7 (98.9)

R merge (%)

10.4 (61.1)

7.7 (90.2)

I/σ (I)

14.2 (1.6)

23.7 (2.6)

CC 1/2

0.998 (0.777)

0.999 (0.801)

Refinement statistics

Resolution (Å)

20.0–2.40

20.0–2.50

R work/R free (%)

23.3/28.1

22.0/27.0

Number of non-Hydrogen atoms

  

Protein [Fc(A)/Fc(B)/FcR(C)]

1700/1712/1225

1714/1714/1225

Water

109

109

Sugar [Fc(A)/Fc(B)/FcR(C)]

110/110/63

110/110/78

R.m.s. deviations from ideal

Bond lengths (Å)

0.010

0.011

Bond angles (°)

1.57

1.61

Ramachandran plot (%)

Most favored regions

93.4

91.2

Additionally allowed regions

6.2

8.6

Generously allowed regions

0.4

0.2

Disallowed

0

0

Average B-factors (Å2)

Protein [Fc(A)/Fc(B)/FcR(C)]

56.6/44.3/70.9

66.8/57.2/81.4

Water

47.3

54.5

Sugar [Fc(A)/Fc(B)/FcR(C)]

67.1/63.5/106.2

77.1/77.1/127.2