Table 1 Crystallographic data collection and refinement statistics.

From: Characterization and structural determination of a new anti-MET function-blocking antibody with binding epitope distinct from the ligand binding domain

 

MET - 107_A07 Fab complex

Data collection

Radiation Source, Beamline

ESRF, ID29

Wavelength (Å)

0.91376

Space group

P22121

Cell dimensions

 a, b, c (Å)

71.88 82.28 267.30

α, β, γ (°)

90, 90, 90

Resolution (Å)

48.95–2.60 (2.74–2.60)1

Rmeas 2

11.1 (88.3)

<I/σ(I)>

11.7 (2.0)

Completeness (%)

99.0 (95.8)

Redundancy

5.5 (5.5)

No. of unique reflections

49,099 (6,685)

Refinement

Resolution (Å)

48.94–2.60

No. of reflections:

 Total

48,940

Rfree set

2,000

Rcryst 3/Rfree 4

21.5/25.7

Contents of asymmetric unit:

 Protein atoms

10,043

Solvent atoms

88

R.m.s deviations:

Bond lengths (Å)

0.005

Bond angles (°)

0.999

  1. 1The statistics shown in parentheses are for the highest-resolution shell.
  2. 2 R meas = (Σ hkl [N/(N-1)]1/2 Σ i |I i (hkl)−I mean (hkl)|)/Σ hkl Σ i I i (hkl), where N is redundancy.
  3. 3 R cryst = Σ hkl ||Fobs(hkl)|−|Fcalc(hkl)||/Σ hkl |Fobs(hkl)|.
  4. 4 R free is the same as R cryst for a random subset not included in the refinement of about 4% of total reflection.
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