Table 1.
Grb7 SH2 domain Data Collection and Refinement Statistics
| Grb7 SH2 | |
| Data Collection | |
| Space group | P212121 |
| Unit Cell (Å) | a = 62.6 |
| b = 63.9 | |
| c = 105.7 | |
| α = β = γ = 90° | |
| Molecules in the ASU | 4 |
| Resolution range (Å)a | 44 – 2.1 (2.18 – 2.1) |
| Observations | 79384 |
| Unique reflections | 25401 |
| Completeness (%)a | 99.1 (99.4) |
| I/σa | 12.6 (2.2) |
| Rmerge (%)a, b | 8.4 (50.5) |
| Wilson B (Å)a | 28.4 |
| Refinement | |
| Resolution limits (Å)a | 30 – 2.10 (2.15 – 2.10) |
| No. of reflectionsa | 23949 (1731) |
| Rcryst (%)a | 20.1 (25.4) |
| Rfree (%)a, c | 25.5 (28.9) |
| Protein atoms | 3733 |
| Water molecules | 181 |
| Other molecules | 7 SO42- |
| r.m.s.d. from ideal values ideaiations | |
| Bond lengths (Å) | 0.014 |
| Bond angles (°) | 1.486 |
| Average B-factors (Å)3 | |
| Protein | 38.1 |
| Water | 40.6 |
| Ions | 58.7 |
aValues in parentheses are for the highest resolution shell happiness
bRmerge = Σ |I – < I >|/Σ I where I is the observed diffraction intensity of the jth observation of reflection hkl and < I > is the average diffraction intensity of all measurements of reflection hkl.
cRfree = Σ | |Fo|-|Fc|/Σ |Fo| where |Fo| and |Fc| are the observed and calculated factors respectively.