| Data collection |
| Wavelength (Å) |
0.999 |
1.0 |
1.1364 |
1.10475 |
0.976 |
1.0703 |
1.2125 |
| Temperature (K) |
100 |
100 |
100 |
100 |
100 |
100 |
100 |
| Space group |
C2 |
C2 |
C2 |
C2 |
C2 |
C2 |
C2 |
| Unit cell parameters |
|
|
|
|
|
|
|
| a, b, c (Å) |
358.4, 88.2, 150.9 |
357.5, 86.8, 150.6 |
360.9, 86.6, 151.0 |
358.8, 88.1, 150.9 |
358.0, 88.9, 151.9 |
358.9, 88.1, 150.9 |
357.4, 87.6, 150.8 |
| β (deg) |
111.9 |
112.6 |
113.2 |
112.0 |
111.8 |
111.9 |
112.6 |
| Resolution (Å)b
|
90–4.4 (4.6–4.4) |
50–5.5 (5.7–5.5) |
100–7.9 (8.1–7.9) |
100–5.5 (5.7–5.5) |
50–6.3 (6.5–6.3) |
50–7.2 (7.5–7.2) |
100–7.2 (7.4–7.2) |
| Reflections |
|
|
|
|
|
|
|
| Unique |
28 079 |
14 396 |
4984 |
14 590 |
9838 |
6610 |
6550 |
| Completeness (%) |
99.3 (99.3) |
99.7 (100) |
99.4 (100) |
99.6 (97.3) |
99.1 (100) |
99.7 (99.2) |
99.5 (95.2) |
| Redundancy |
3.3 (3.5) |
3.6 (3.7) |
6.1 (6.3) |
3.7 (3.7) |
3.7 (3.8) |
7.3 (7.2) |
6.8 (4.8) |
| I/σ(I) |
12.0 (2.0) |
17.7 (1.4) |
13.6 (2.8) |
18.3 (1.5) |
13.1 (1.6) |
23.5 (2.7) |
12.9 (0.7) |
| Rsym(I)c
|
0.054 (0.73) |
0.041 (0.78) |
0.066 (0.79) |
0.082 (0.79) |
0.080 (0.72) |
0.033 (0.73) |
0.051 (0.92) |
| |
|
|
|
|
|
|
|
| Phasing |
| Resolution (Å) |
90–4.4 |
35–5.5 |
50–7.9 |
50–5.5 |
35–6.3 |
47–7.2 |
35.2–7.2 |
| Sites |
|
6 |
2 |
2 |
4 |
1 |
1 |
| Phasing power (acentric)d
|
|
|
|
|
|
|
|
| Isomorphous |
|
0.65 |
0.47 |
0.28 |
0.45 |
0.57 |
0.61 |
| Anomalouse
|
|
0.20 |
0.39 |
0.10 |
0.17 |
0.20 |
0.21 |
| RCullis (acentric)f
|
|
|
|
|
|
|
|
| Isomorphous |
|
0.63 |
0.78 |
0.60 |
0.74 |
0.72 |
0.71 |
| Anomalous |
|
0.99 |
0.98 |
0.99 |
0.99 |
0.99 |
0.98 |
| FOMg
|
0.56 |
|
|
|
|
|
|
| |
|
|
|
|
|
|
|
| Refinement |
| Resolution (Å) |
90–4.4 |
|
|
|
|
|
|
| Reflections |
|
|
|
|
|
|
|
| Number |
28 077 |
|
|
|
|
|
|
| Completeness (%) |
99.3 |
|
|
|
|
|
|
| Test set (%) |
5.0 |
|
|
|
|
|
|
| Rhwork
|
0.299 |
|
|
|
|
|
|
| Rhfree
|
0.348 |
|
|
|
|
|
|
| Contents of A.U. |
|
|
|
|
|
|
|
| Protein residues |
1716 |
|
|
|
|
|
|
| Nucleic acid residues |
346 |
|
|
|
|
|
|
| Ramachandran ploti
|
|
|
|
|
|
|
|
| Favoured |
85.8 |
|
|
|
|
|
|
| Allowed |
11.6 |
|
|
|
|
|
|
| Outliers |
2.6 |
|
|
|
|
|
|
| r.m.s.d. Geometry |
|
|
|
|
|
|
|
| Bond lengths (Å) |
0.004 |
|
|
|
|
|
|
| Bond angles (deg) |
1.201 |
|
|
|
|
|
|
| Abbreviations: A.U., asymmetric unit; r.m.s.d., root-mean-square deviation. |
|
aPIP—[Pt2I2(H2NCH2CH2NH2)2]. |
|
bData for the highest resolution shell in parentheses. |
|
cRsym(I)=ΣhklΣI∣Ii(hkl)−〈I(hkl)〉∣/ΣhklΣi∣Ii(hkl)∣; for n independent reflections and i observations of a given reflection, where 〈I(hkl)〉=average intensity of the i observations. |
|
dPhasing power=∣FH,calc∣/Σhkl∣∣FPH±FP∣−∣FPH,calc∣∣. |
|
eAlthough the anomalous signals were weak, they were included in phasing and visibly improved the electron density. |
|
fRCullis=Σhkl∣∣FPH±FP∣−∣FPH,calc∣∣/Σhkl∣FPH−FP∣. |
|
gFOM=mean figure of merit=〈cos(αbest−αcalc)〉, where α=phase angle. |
|
hR=Σhkl∣∣Fobs∣−∣Fcalc∣∣/Σhkl∣Fobs∣, where Rwork=hkl∉T; Rfree=hkl∈T; Rall=all reflections; T=test set. |
|
iCalculated with MolProbity (http://molprobity.biochem.duke.edu/). |
