Table 1. Data-collection and processing statistics for the rat FGF1–SOS–FGF1 complex.
Values in parentheses are for the highest resolution shell.
| X-ray source | BW7A, EMBL, Hamburg |
| Wavelength (Å) | 0.8142 |
| Space group | P21 |
| Unit-cell parameters | |
| a (Å) | 36.88 |
| b (Å) | 52.78 |
| c (Å) | 73.13 |
| β (°) | 97.43 |
| Mosaicity (°) | 0.7 |
| Resolution (Å) | 40.8–2.2 (2.32–2.20) |
| No. of observations | 41588 |
| No. of unique reflections | 12293 |
| Redundancy | 3.4 |
| Completeness (%) | 98.4 (98.2) |
| 〈I/σ(I)〉 | 16.7 (7.0) |
| Rmerge† (%) | 5.1 (19.2) |
| VM (Å3 Da−1) | 2.39 |
| Refinement | |
| Protein atoms | 2143 |
| Protein residues | |
| Chain A | 7–138 |
| Chain B | 8–138 |
| Other atoms | 163 waters, 1 sucrose octasulfate (55 atoms) |
| Rwork‡ (%) | 20.6 |
| Rfree§ (%) | 27.7 |
| Mean B values (Å2) | |
| Molecule A | |
| Main chain | 15.3 |
| Side chain | 23.0 |
| Molecule B | |
| Main chain | 22.7 |
| Side chain | 27.4 |
| Water atoms | 25.6 |
| Sucrose octasulfate atoms | 20.0 |
| R.m.s.d. bond lengths (Å) | 0.022 |
| R.m.s.d. bond angles (°) | 1.5 |
†
R
merge = 
, where I
i(hkl) is the intensity of an individual measurement of the reflection with Miller indices hkl and 〈I(hkl)〉 is the mean intensity of that reflection.
‡
R
work = 
, where |F
o,hkl| and |F
c,hkl| are the observed and calculated structure-factor amplitudes, respectively.
§
R free is equivalent to R work, but calculated with reflections omitted from the refinement process (5% of reflections were omitted).