Table 1. Diffraction Data Collection and Structure Refinement Statistics.
| Data Collectiona | ||||||
|---|---|---|---|---|---|---|
| Crystal | IpaB28.226 | IpaB28.226 | IpaB28.226 | SipB30.237 | SipB30.237 | |
| Native | Pt Remote | Pt Peak | SeMet Remote | SeMet Peak | ||
| Beamline | APS 22-BM | APS 22-BM | APS 22-BM | APS 22-BM | APS 22-BM | |
| Space Group | P21 | P21 | P21 | P21212 | P21212 | |
| Unit Cell Dimensions | ||||||
| a (Å) | 52.391 | 52.300 | 52.300 | 51.144 | 51.052 | |
| b (Å) | 28.372 | 28.060 | 28.060 | 84.646 | 84.715 | |
| c (Å) | 104.804 | 104.760 | 104.760 | 159.155 | 159.336 | |
| β(°) | 95.966 | 95.920 | 95.920 | |||
| Wavelength (Å) | 1.0000 | 1.0000 | 1.0719 | 0.9724 | 0.9793 | |
| Resolution (Å) | 50-2.1 | 50-2.5 | 50-2.5 | 50-2.8 | 50-3.0 | |
| Completeness (%) | 91.7 (59.3) | 95.7 (72.0) | 97.2 (80.5) | 98.0 (87.2) | 99.2 (95.5) | |
| Reflections (total) | 61,832 | 68,016 | 71,247 | 209,952 | 86,789 | |
| Reflections (unique) | 18,186 | 10,464 | 10,634 | 17,478 | 14,590 | |
| Redundancy (fold) | 3.4x | 6.5x | 6.7x | 12.0x | 5.9x | |
| <I>/<σI> | 13.4 (2.0) | 18.6 (2.82) | 19.4 (3.6) | 18.8 (2.55) | 14.3 (2.05) | |
| Rmerge (%)b | 8.5 (42.5) | 8.4 (35.0) | 8.2 (27.8) | 10.0 (67.1) | 11.5 (61.1) | |
| Refinement | ||||||
| RCSB Accession Code | 3U0C | 3TUL | ||||
| Protein Molecules/AU | 2 | 4 | ||||
| Rwork/Rfree (%)c | 24.53/29.45 | 29.73/31.67 | ||||
| Number of Atoms | ||||||
| Protein | 2426 | 3877 | ||||
| Solvent | 88 | 43 | ||||
| Ramachandran Plot (%) | ||||||
| Favored | 97.7 | 95.7 | ||||
| Allowed | 0.6 | 4.0 | ||||
| Outliers | 1.7 | 0.2 | ||||
| RMSD | ||||||
| Bond | ||||||
| Lengths (Å) | 0.008 | 0.009 | ||||
| Bond | ||||||
| Angles (°) | 1.066 | 1.240 | ||||
| B factor (Å2) | ||||||
| Protein | 44.76 | 52.56 | ||||
| Solvent | 50.60 | 58.10 |
Numbers in parentheses are for the highest-resolution no.
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.
R = Σh|Fobs(h)-Fcalc(h)|/Σh|Fobs|. Rcryst and Rfree were calculated from the working and test reflection sets, respectively. The test set constituted 5% of the total reflections not used in refinement.
Procedures detailing crystallization and data collection of IpaB28.226 and SipB30.237 are detailed in Supplementary Material. Briefly, crystals of both proteins were obtained by the hanging drop vapor diffusion method. Following data collection, individual reflections were indexed, integrated, and scaled using HKL2000 49. Both structures were determined by two-wavelength MAD phasing using the program AutoSol within the PHENIX suite 50. The experimental models were iteratively improved by manual building in Coot 51; 52, and refined using phenix.refine within the PHENIX suite 50.