Table 2 Data collection and refinement statistics

From: Structure of Myosin VI/Tom1 complex reveals a cargo recognition mode of Myosin VI for tethering

Data set

Myosin VI/Tom1 complex

Data collection

 

 Space group

P1211

 Unit cell parameters

 

   a, b, c (Å)

40.73, 74.88, 50.87

   α, β, γ (o)

90, 106.34, 90

 Wavelength (Å)

0.97774

 Resolution range (Å)

50.00–1.80 (1.83–1.80)

 Number of total reflections

177,263

 Number of unique reflections

26915

 Redundancy

6.60 (6.20)

 I/σΙ

28.14 (4.74)

 Completeness (%)

98.50 (98.50)

 Rmerge (%) a

5.60 (35.40)

Structure refinement

 

 Resolution (Å)

37.44–1.80(1.87–1.80)

 Rworkb/Rfreec (%)

17.66/23.35

 Number of reflections

 

   Working set

25,194

   Test set

1252

 B factor (Å2)

 

   Average

31.37

   Protein

30.99

 RMSD bonds (Å)

0.01

 RMSD angles (o)

1.16

 Number of non-hydrogen atoms

 

   Protein

2281

   Ligand

0

   Water

249

Ramachandran plot (%)

 

  Most favored

99.24

  Additionally allowed

0.76

  Outliers

0

  1. aRmerge = Σ|I-<I>|/Σ<I>, where I is the intensity of the measured reflection,<I> is the mean intensity of all symmetry-related reflections. Values in parentheses are for highest-resolution shell
  2. bRwork = Σ||Fobs| − |Fcal||/Σ|Fobs|, where Fobs and Fcal are observed and calculated structure factors
  3. cRfree = ΣT||Fobs| − |Fcal||/ΣT|Fobs|, where T is a randomly chosen test data set of about 5% of the total reflections and set aside prior to refinement. Values in parentheses are for the highest-resolution shell
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