Table 1.
X-ray data collection statistics (values in parentheses refer to the highest resolution shell)
| Protein | M. tuberculosis |
K. pneumoniae FAD |
K. pneumoniae FADH− |
|---|---|---|---|
| Data collection | ESRF ID14-2 | Inhouse | FADH- |
| Wavelength (Å) | 0.933 | 1.54178 | 1.54178 |
| Spacegroup | P21212 | P3221 | P3221 |
| Resolution (Å) | 24.5-2.25 (2.37-2.25) |
39.2-2.00d (2.12-2.00)d |
28.1-2.35 (2.48-2.35) |
| Cell (Å) | a=137.6, b=153.73, c=137.68 α=β=γ=90.0° |
a=85.7, b=85.7, c=99.8 α=β=90°, γ=120.0° |
a=86.0, b=86.0, c=100.8 α=β=90°, γ=120.0° |
| Unique reflections | 1188969 | 24352 | 17405 |
| I/σ | 23 (1.1) | 25 (4.3) | 12 (1.9) |
| Multiplicity | 6.2 (5.3) | 17 (9.1) | 2.5 (2.5) |
| Data completeness (%) | 89 (85.2) | 88 (49)d | 100(99.1) |
| Rmerge (%)a | 10.2 (61.4) | 4.6 (17.7) | 6.4 (47.9) |
| Refinement | |||
| Rfactorb (%) | 24.2 (34.9) | 19.3 (29.0) | 18.7 (27.6) |
| Rfreec (%) | 28.3 (36.1) | 24.7 (34.1) | 24.3 (34.1) |
| Rmsd bond distances (Å) | 0.014 | 0.010 | 0.011 |
| Rmsd angle ° | 1.453 | 1.203 | 1.230 |
| In Ramachandran % Core e % disallowed e |
91 0 |
91 0 |
89 0 |
| PDB code31 | 1VOJ | 2B17 | 1USJ |
Rmerge = Σhkl Σl|Ii − <I>|/ Σhkl Σl <I>, where Ii is an intensity for the ith measurement of a reflection with indices hkl and <I> is the weighted mean of the reflection intensity.
Rfactor = Σhkl|Fo(hkl)| − |Fc(hkl)||/ Σhkl| Fo(hkl)|, where Fo and Fc are the observed and calculated structure factors, respectively.
Rfree is the crystallographic Rfactor calculated with 5% of the data that were excluded from the structure refinement.
Data extend to 2.0Å and were used in refinement. Due to a technical problem with the detector which prevented its distance being changed, these data were collected in the corners and are incomplete. The structure is quoted to 2.2Å as this is the last shell (2.3Å-2.2Å) where completeness is 90% and the overall completeness to 2.2Å is 98%.
Core and disallowed areas are defined by PROCHECK32.