Table 1.
X-ray crystallography data
| Statistic | Data set
|
||
|---|---|---|---|
| Native | kAu (CN)2 | HgI2 | |
| Data collection and phasing | |||
| Resolution (Å) | 2.3 | 2.5 | 2.5 |
| Reflection, unique/total | 24,024/104,060 | 20,666/120,404 | 20,699/117,909 |
| Data completeness (%); overall (final shell) | 93.9 (83.4) | 97.2 (96.2) | 96.7 (92.3) |
| Heavy-atom concentration | — | 1 mM | 20% |
| Soaking time, days | — | 2 | 2 |
| Rmerge* (%) (final shell) | 7.0 (36.2) | 7.1 (34.3) | 10.0 (41.8) |
| Riso† (%) | — | 12 | 11 |
| Heavy-atom binding site | — | 1 | 2 |
| Rcullis‡, 15–3.0 Å | — | 0.70 | 0.74 |
| Phasing power§, centric/acentric | — | 1.11/1.05 | 0.91/1.13 |
| Refinement | |||
| Resolution (Å) | 8–2.3 | ||
| R-factor (%) | 18.5 | ||
| Rfree (%) | 25.8 | ||
| Observation F > 2σ (F) | 23,447 | ||
| Total number of protein atoms | 3,515 | ||
| Total number of water molecules | 184 | ||
| rmsd bond lengths (Å) | 0.012 | ||
| rmsd bond angles (degree) | 1.348 | ||
rmsd, root-mean-square deviation.
*
Rmerge = ∑∑j|Ij − 〈I〉|/∑〈I〉.
†
Riso = ∑∥Fph|−|Fp∥/∑|Fp|.
‡
Rcullis = lack of closure/isomorphous difference.
§
Phasing power = FH/lack of closure.