TABLE 1.
Crystallographic data for MsTsf1
| MsTsf1 (K2PtCl4) | MsTsf1 (native) | |
|---|---|---|
| Data collection | ||
| Unit‐cell parameters (Å, o) | a = 65.61, b = 141.42, c = 150.40 | a = 64.49, b = 139.06, c = 146.70 |
| Space group | P212121 | P212121 |
| Resolution (Å) a | 49.44–2.85 (2.99–2.85) | 47.28–2.05 (2.09–2.05) |
| Wavelength (Å) | 1.0000 | 1.0000 |
| Temperature (K) | 100 | 100 |
| Observed reflections | 545,842 | 544,369 |
| Unique reflections | 33,530 | 83,612 |
| <I/σ (I)> a | 10.8 (2.1) | 7.6 (2.2) |
| Completeness (%) a | 99.9 (99.6) | 100 (100) |
| Multiplicity a | 16.3 (17.1) | 6.5 (6.6) |
| R merge (%) a , b | 24.1 (187.2) | 16.2 (82.7) |
| R meas (%) a , c | 24.9 (193.0) | 17.6 (89.8) |
| R pim (%) a , c | 6.2 (46.6) | 6.9 (34.8) |
| CC1/2 a , d | 0.997 (0.777) | 0.991 (0.697) |
| DelAnom CC e | 0.481 (0.039) | — |
| Refinement | ||
| Resolution (Å) a | 40.00–2.05 | |
| Reflections (working/test) a | 79,455/4,065 | |
| R factor/R free (%) a , f | 20.9/27.2 | |
| No. of atoms (Protein/Fe3+/CO3/water) | 9,925/2/16/422 | |
| Model quality | ||
| R.m.s deviations | ||
| Bond lengths (Å) | 0.008 | |
| Bond angles (o) | 0.964 | |
| Average B‐factor (Å b ) | ||
| All Atoms | 33.4 | |
| Protein | 33.5 | |
| Fe3+ | 18.7 | |
| CO3 | 22.6 | |
| Water | 49.3 | |
| Coordinate error (maximum likelihood) (Å) | 0.30 | |
| Ramachandran plot | ||
| Most favored (%) | 94.8 | |
| Additionally allowed (%) | 4.6 |
Values in parenthesis are for the highest resolution shell.
R merge = ∑hkl∑i|I i(hkl) − <I(hkl)>|/∑hkl∑i I i(hkl), where I i(hkl) is the intensity measured for the ith reflection and <I(hkl)> is the average intensity of all reflections with indices hkl.
R meas = redundancy‐independent (multiplicity‐weighted) R merge. 52 , 70 R pim = precision‐indicating (multiplicity‐weighted) R merge. 71 , 72
CC1/2 is the correlation coefficient of the mean intensities between two random half‐sets of data. 73 , 74
DelAnom CC is the correlation coefficient between the Bijvoet differences (I (hkl) – I (−h‐k‐l)) from two random half‐sets of data 52 and is used to estimate the anomalous signal strength.
R factor = ∑hkl||F obs (hkl)| − |F calc (hkl)||/∑hkl|F obs (hkl)|; R free is calculated in an identical manner using 5% of randomly selected reflections that were not included in the refinement.