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Table 2 X-ray diffraction data and refinement statistics

From: Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6

A. X-ray Data

 

X-ray Source

SSRL

 

Beam line 7–1

Space Group

I 432

Cell Dimensions

 

a = b = c (Å)

181.0

Asymmetric Unit

1 monomer

Resolution Range (Ã…)

27.9–1.55

 

(1.63–1.55)

R merge

0.067

 

(0.767)*

R p.i.m. *

0.013

 

(0.25)

mean (I/σ(I))

29.4

 

(3.8)

Multiplicity

24.7

 

(17.8)

No. Unique Reflections

72,486

 

(10,350)

Data Completeness (%)

99.9

 

(99.1)

B. Refinement

 

R work

0.1267

R free

0.1552

Bonds (Ã…)

0.008

Angles (Ëš)

1.562

No. Amino Acids

391

No. Glycan monomers

15

No. D-glucose molecules

4

No. Waters

458

  1. (Statistics for the highest resolution shell are in parentheses).
  2. *R merge is high in the highest resolution shell due to the high multiplicity of the data. The R p.i.m. is independent of the data multiplicity and shows that the data in the highest shell have a reasonable discrepancy of 25%. R p.i.m. is the precision indicating R merge [27].