Table 3 Summary of crystallographic structure determination statistics

From: Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation

Data collection statistics

mVps29 – hDENND4C1189-1206

PDB ID

8VOD

Beamline

MX2

Space group

P 32 2 1

Resolution (Å)

34.13 – 2.35

 

(2.43 – 2.35)

a, b, c (Å)

42.90, 42.90, 172.74

α, β, γ (°)

90.00, 90.00, 120.00

Data collection temp. (K)

100

Wavelength (Å)

0.95365

Total observations

16,359 (1561)

Unique reflections

8279 (785)

Completeness (%)

99.7 (100.0)

Rmerge+

0.028 (0.195)

Rpim*

0.028 (0.195)

CC1/2

0.998 (0.891)

<I/σ(I)>

9.87 (2.35)

Multiplicity

2.0 (2.0)

Molecule/asym

1

Refinement statistics

Rwork/Rfree (%)#

18.78/25.22

No. protein atoms

1590

Waters

26

Wilson B (Å2)

49.33

Average B (Å2)^

53.92

Protein

53.84

Water

48.12

rmsd bonds (Å)

0.008

rmsd angles (°)

1.07

Ramachandran plot:

Favoured/outliers (%)

95.38/0.51

  1. Values in parentheses refer to the highest resolution shell. +Rmerge = Σ|I – <I > | ⁄ Σ<I > , where I is the intensity of each individual reflection. *Rpim indicates all I+ & I. Rwork = Σh|Fo - Fc | / Σl | Fo | , where Fo and Fc are the observed and calculated structure-factor amplitudes for each reflection h. #Rfree was calculated with 10% of the diffraction data selected randomly and excluded from refinement. ^Calculated using Baverage.