Table 1.
Data collection and refinement statistics
| Crystal | FIXa EGF2/Protease domain |
|---|---|
| PDB code | 6MV4 |
| Space Group | I4122 |
| Unit cell parameters | |
| a (Å) | 109.75 |
| b (Å) | 109.75 |
| c (Å) | 112.45 |
| α, β, γ (°) | 90.0, 90.0, 90.0 |
| Data Collection | |
| Beam line | ESRF, ID14-3 |
| Wavelength (Å) | 0.93 |
| Resolution (Å) | 78.54 -1.37 |
| Molecules per asymmetric unit | 1 |
| Measured reflections | 337283 |
| Unique Reflections | 49105 |
| %Completeness (spherical) | 68.3 (12.1) |
| %Completeness (ellipsoidal) | 99.45(99.55) |
| Multiplicity* | 6.9 (5.2) |
| CC(1/2) | 1.0 (0.85) |
| Rmergea | 3.5(46.2) |
| Average I/σ(I) | 26.7(2.7) |
| Wilson B-factor | 18.6 |
| Refined statistics | |
| Resolution (Å) | 1.37 |
| No. of non-H atoms | |
| Total | 2854 |
| Protein | 2360 |
| Ligand/ion | 56 |
| Water | 438 |
| R-factor (%)b | 17.8 |
| Rfree (%)b | 21.0 |
| r.m.s.d. from ideal values | |
| Bond Lengths (Å) | 0.012 |
| Bond Angles (°) | 1.23 |
| Ramachandran plot (%) | |
| Most favored regions (%) | 83.9 |
| Additional allowed regions (%) | 13.7 |
| Generously allowed regions (%) | 0.4 |
| Disallowed regions (%) | 0.0 |
Values in the parenthesis are for the high resolution shell. ESRF, European Synchrotron Radiation Facility.
a
Rmerge=ΣhklΣi|Ii(hkl)−〈I(hkl)〉|/ΣhklΣiIi(hkl), where 〈I(hkl)〉 is the mean intensity of reflection hkl.
b
R-factor=Σhkl||Fobs|−|Fcalc||/Σhkl|Fobs|, where Fobs and Fcalc are the observed and calculated structure factors, respectively; Rfree is the same as the R-factor but is calculated for 10% of randomly selected reflections excluded from the refinement.