Table 1.
Diffraction Data Collection and Structure Refinement Statistics
| Data Collectiona | ||
| Crystal | Ef mvaS | Ef mvaS + hymeglusin |
| Beamline | APS 22-BM | APS 22-BM |
| Wavelength (Å) | 1.000 | 1.000 |
| Space Group | P21 | P21 |
| Cell Dimensions (Å, °) | a=109.53 | a=108.33 |
| b=56.28 | b=52.76 | |
| c=123.89 | c=117.58 | |
| β=100.02 | β=99.51 | |
| Resolution (Å) | 50.00–1.60 | 50.00–1.95 |
| Reflections (unique) | 1,306,891 (193,904) | 445,318 (92,792) |
| Completeness (%) | 98.5 (95.8) | 96.8 (87.3) |
| Redundancy (fold) | 6.7 | 4.8 |
| <I>/<σI> | 22.2 (3.6) | 11.3 (2.6) |
| Rmerge (%)b | 6.2 (45.6) | 12.7 (42.1) |
| Refinement | ||
| RCSB Accession Code | 3V4N | 3V4X |
| Protein Molecules/AU | 4 | 4 |
| Rwork/Rfree (%)c | 14.1/19.4 | 17.1/21.8 |
| Number of Atoms | ||
| Protein | 11,975 | 11,862 |
| Ligand | n/a | 92 |
| Solvent | 1,494 | 1087 |
| RMSD | ||
| Bond Length (Å) | 0.003 | 0.010 |
| Bond Angle (°) | 0.72 | 1.25 |
| B factor (Å2) | ||
| Protein | 27.7 | 19.74 |
| Ligand | n/a | 32.34 |
| Solvent | 35.9 | 24.95 |
| Coordinate Error (Å) | 0.400 | 0.200 |
| Phase Error (°) | 20.3 | 21.8 |
| Ramachandran Plot (%) | ||
| Favored | 97.7 | 97.4 |
| Allowed | 2.3 | 2.6 |
| Outliers | 0.0 | 0.0 |
a
Numbers in parentheses are for the highest-resolution shell.
b
Rmerge = ΣhΣi|Ii(h)−<I(h)>|/ ΣhΣiIi(h), where Ii(h) is the ith measurement of reflection h and <I(h)> is a weighted mean of all measurements of h.
c
R=Σh|Fobs(h)−Fcalc(h)|/ ΣhΣFobs|. Rcryst and Rfree were calculated from the working and test reflection sets, respectively. The test set constituted 10% of the total reflections not used in refinement.