Table 1 X-ray diffraction data collection and refinement statistics for RfCohScaB5-DocScaA.

From: Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction

Data collection

Beamline

PROXIMA-1, Soleil

Space Group

P1211

Wavelength (Å)

0.82

Unit-cell parameters

    a, b c (Å)

30.09, 142.90, 46.59

    α, β, γ (°)

90, 90.75, 90

VM♯ (Å3 Da−1)

1.89

Solvent Content (%)

35

Resolution limits (Å)

46.58–1.98 (2.07–1.98)

No. of observations

182195 (13279)

No. of unique observations

26476 (2602)

Multiplicity

6.9 (6.9)

Completeness (%)

99.9 (99.7)

<I/σ(I)>

8.85 (3.96)

CC1/2†

0.995 (0.974)

Wilson B-factor

22.71

Rmerge‡

0.098 (0.294)

Rp.i.m.¥

0.037 (0.085)

Structure refinement

R-work§, R-free¥

0.182, 0.214

No. of non-H atoms

3519

    Macromolecules

3287

    Ligands

7

    Water

225

Protein residues

449

RMS(bonds)

0.010

RMS(angles)

1.4

Ramachandran favored (%)

96

Ramachandran outliers (%)

0

Clash score

0.61

Average B-factor

33.80

    macromolecules

33.80

    ligands

39.30

    solvent

33.50

PDB accession code

5N5P

  1. Values in parenthesis are for the highest resolution shell.
  2. #Matthews coefficient50.
  3. †CC1/2 = the correlation between intensities from random half‐dataset (Diederichs & Karplus, 2013).
  4. ‡R merge  = Σ hkl Σ i |I i (hkl) − <I(hkl)>|/Σ hkl Σ i I i (hkl), where I i (hkl) is the ith intensity measurement of reflection hkl, including symmetry-related reflections and <I(hkl)> is its average.
  5. ¥\({R}_{p.i.m.}=\frac{{\sum }_{hkl}\sqrt{1/(n-1)}{\sum }_{i=1}^{n}|{I}_{i}(hkl)-I^{\prime} (hkl)|}{{\sum }_{hkl}{\sum }_{i=1}^{n}{I}_{i}(hkl)}\), a redundancy-independent version of Rmerge.
  6. §Rwork = Σ hkl ||F obs | − |F calc ||/Σ hkl |F obs |; ¥R free as R work , but summed over a 5% test set of reflections.
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