Skip to main content

Table 1 Data collection, phasing and refinement statistics.

From: X-ray structures of two proteins belonging to Pfam DUF178 revealed unexpected structural similarity to the DUF191 Pfam family

 

Se -SAD (10093b)

Se -SAD (10093f)

Cell dimensions

a = 75.3,b = 139.4, c = 153.6; β = 92.8°

a = 75.8,b = 97.4, c = 86.6; β = 106.5°

Space group

P21

P21

Data Collection Statistics

  

Wavelength (Ã…)

0.98

0.98

Temperature (K)

100

100

Resolution range

50.0-2.5

50-2.04

Outermost Shell (Ã…)

2.59-2.5

2.11-2.04

Unique reflections

107665 (9866)

76032(6908)

Completeness (%)

98.9(91.0)

98.8(89.7)

Mean I/σ(I)

11.1 (1.9)

16.8(2.1)

Redundancy

6.8(5.2)

4.6(3.9)

Rmerge 1

0.095(0.40)

0.043(0.21)

Phasing Statistics

  

Phasing power2 (ano)

0.83

0.94

FOM3:

0.29

0.27

After density modification

0.93

0.92

Refinement Statistics

  

No. of reflections (work)

100602

71996

No. of reflections (test)

3150

2264

4Rfactor/5Rfree

0.20/23.4

0.24/0.28

Resolution range (Ã…)

50.0-2.5

30.0-2.04

RMSD for bond length (Ã…)

0.006

0.006

RMSD bond angles (°)

1.35

1.4

<B-values>

  

Main-chain (Ã… 2)

30.8

30

Side-chain (Ã… 2)

32.4

32.4

Number of non-H atoms

  

No. of heteroatoms

90

0

No of water molecules

653

579

  1. Values for the highest resolution shell are given within parentheses.
  2. 1Rmerge = Σ|Ii-⟨I⟩|/Σ|Ii| where Ii is the intensity of the ith measurement, and ⟨I⟩ is the mean intensity for that reflection.
  3. 2Phasing power and 3FOM (Figure of merit) as defined in SHARP.
  4. 4Rfactor = Σ||Fobs|-|Fcalc||/Σ|Fobs| where |Fcalc| and |Fobs| are the calculated and observed structure factor amplitudes, respectively.