Table 1 Data collection, MAD phasing, and refinement statistics.

From: Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation

 

Native

Se-Met (Hsp104MMM)

Data Collection Statistics

Space group

P 6522

P 6522

Unit Cell

a = 179.1 Å, b = 179.1 Å, c = 69.7 Å

a = 179.5 Å, b = 179.5 Å, c = 69.1 Å

 

α = 90°, β = 90°, γ = 120°

α = 90°, β = 90°, γ = 120°

Source

NSLS-X25

NSLS-X25

Wavelength (Å)

λ = 1.10

λ1 = 0.9789

λ2 = 0.9792

λ3 = 1.0024

Resolution (Å)

41.53–2.82

44.8–3.5

44.8–3.5

44.8–3.8

Completeness (%)a

84.2 (12.7)

99.8 (100)

99.8 (99.5)

99.9 (99.9)

Redundancy

14.7 (1.7)

6.9 (6.8)

6.9 (6.5)

6.7 (6.9)

Rsym a,b

0.076 (0.386)

0.086 (0.393)

0.091 (0.497)

0.088 (0.320)

I/σc

17.6

12.9

11.1

10.7

MAD Phasing Statistics

Riso d

0.222

 

0.044

0.053

RCullis e

  

0.62

0.72

Phasing Powerf

 

2.38

2.07

1.16

Figure of Meritg

 

0.63 (centric)

0.60 (acentric)

 

Refinement Statistics

Resolution (Å)

41.53–2.82

   

No. reflections

14036

   

Rcryst/Rfree

0.210/0.279

   

No. atoms

2725

   

Protein

2721

   

Water

4

   

B-factors

94.1

   

Protein

94.1

   

Water

74.3

   

rmsd bond (Å)

0.002

   

rmsd angle (°)

0.399

   

Ramachandran

Favored (%)

97.1

   

Outliers (%)

0.0

   
  1. aValues for the highest resolution shell are given in parentheses. bRsym = Σhkl|I(hkl) − < I(hkl) > |/ΣhklI(hkl), where <I(hkl)> is the mean of the symmetry equivalent reflections of I(hkl). cBased on unmerged data. dRiso = Σ|FPH − FP|/ΣFp, where Fp is the peak (λ1), and FPH are the inflection (λ2), low energy remote (λ3) or native structure factor amplitudes. eRCullis = Σ||FPH ± FP| − FH calc|/Σ|FPH ± FP| for centric reflections only. fIsomorphous phasing power = Σ|FH|/Σ||FPH obs| − |FPH calc||; anomalous phasing power = Σ|F″H|/Σ||ADobs| − |ADcalc||. gFigure of Merit = weighted mean of the cosine of the deviation from αbest.
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