Table 2 |
|
|
Crystallographic data and refinement statistics |
|
|
X-ray diffraction data |
|
|
Space group |
C2 |
|
Unit Cell Dimensions: a, b, c (Å) α, β, γ (°) |
162.0, 66.4, 93.6 90, 98.2, 90 |
|
Wavelength (Å) |
1.0088 |
|
Resolution Range (Å) |
19.34 - 2.75 (2.90 - 2.75)* |
|
Rsym (%) |
7.0 (36.2) |
|
I/σ |
19.92 (4.42) |
|
Measured reflections |
64394 (9470) |
|
Unique reflections |
22267 (3362) |
|
Redundancy |
2.89 (2.82) |
|
Completeness (%) |
86.0 (88.8) |
|
|
|
|
Refinement |
|
|
Resolution (Å) |
19.34 - 2.75 |
|
Rcryst/Rfree (%) |
23.8/29.2 |
|
Atoms (protein/ligand/solvent) |
5469/56/243 |
|
Rmsd bond length (Å) |
0.012 |
|
Rmsd bond angles (°) |
1.6 |
|
Average B-factors (Å2, main chain/side chain) |
66.4 |
|
|
|
|
* Data in parentheses represent the highest resolution shell. Deposited under PDB 3L1C. |
|
|
Heuston et al. BMC Structural Biology 2010 10:19 doi:10.1186/1472-6807-10-19 |
|
