Table 2.
Crystallographic data collection and model refinement statistics for the crystal structures of BH1352 (wildtype and K184L) and E. coli DeoC (EcDERA)
| Structure | apo BH1352 | apo BH1352 K184L | EcDERA |
|---|---|---|---|
| PDB code | 6D33 | 6MSW | 1KTN |
| Data collection | |||
| Space group | C2 | C2 | C2 |
| Cell dimensions | |||
| a, b, c (Å) | 240.91, 55.52, 177.71 | 240.78, 55.13, 176.30 | 62.57, 53.56, 81.36 |
| α, β, γ (°) | 90, 128.02, 90 | 90, 127.71, 90 | 90, 109.97, 90 |
| Resolution, Å | 30.0–2.50 | 30.0–2.17 | 50.0–1.40 |
| Rmergea,b | 0.049 (0.654) | 0.077 (0.734) | 0.078 (0.309) |
| Rpim | 0.027 (0.392) | 0.042 (0.405) | —c |
| CC½d | 0.750 | 0.815 | —c |
| I/σ(I) | 34.2 (2.56) | 17.8 (2.11) | 20.0 (2.44) |
| Completeness, % | 98.9 (97.5) | 100 (100) | 99.5 (98.2) |
| Redundancy | 3.9 (3.5) | 4.2 (4.2) | 6.0 (4.5) |
| Refinement | |||
| Resolution, Å | 30.02–2.50 | 29.98–2.17 | 38.65–1.40 |
| No. of unique reflections: working, test | 63,680, 1,995 | 97,396, 1,997 | 88731, 4,458 |
| R factor/free R factore | 20.4/25.0 (29.7/32.9) | 19.3/21.1 (28.8, 30.0) | 18.6/20.5 (18.7/19.9) |
| No. of refined atoms, molecules | |||
| Protein | 9,557, 6 | 9,514, 6 | 3,763, 2 |
| Solvent | 116, 18 | 102, 17 | N/A |
| Water | 461 | 843 | 631 |
| B-factors | |||
| Protein | 74.70 | 56.58 | 8.54 |
| Solvent | 97.53 | 85.32 | N/A |
| Water | 64.25 | 54.92 | 20.50 |
| RMSD | |||
| Bond lengths, Å | 0.004 | 0.004 | 0.004 |
| Bond angles, ° | 0.632 | 0.618 | 1.300 |
aRsym = ΣhΣi Ii(h) − I(h)/ΣhΣiIi(h), where Ii(h) and I(h) are the ith and mean measurement of the intensity of reflection h.
b The figures in parentheses indicate the values for the outer shells of the data.
c Value not measured.
d Value refers to the outer shells of the data.
e r = Σ|Fpobs − Fpcalc|/ΣFpobs, where Fpobs and Fpcalc are the observed and calculated structure factor amplitudes, respectively.