Table 1. Summary of crystal parameters, data-collection and refinement statistics from crystal forms I and II of Mn-SODDr .
Values in parentheses are for the highest resolution shell.
| Crystal form I | Crystal form II | |
|---|---|---|
| Data collection and processing | ||
| Unit-cell parameters (Å, °) | a = 44.28, b = 83.21, c = 59.52, β = 110.18 | a = 43.57, b = 87.10, c = 116.42, β = 92.1 |
| Space group | P21 | P21 |
| Wavelength (Å) | 0.933 | 0.933 |
| Resolution range (Å) | 29.4–2.2 (2.32–2.2) | 41.2–2.0 (2.11–2.0) |
| No. of observations | 69134 (9955) | 452450 (26160) |
| No. of unique reflections | 20567 (2982) | 48281 (3564) |
| Completeness† (%) | 99.8 (99.8) | 82.2 (41.7) |
| Rsym (%) | 5.7 (16.5) | 7.5 (14.5) |
| 〈I/σ(I)〉 | 15.6 (6.0) | 31.8 (9.0) |
| Multiplicity | 3.4 (3.3) | 9.4 (7.3) |
| Final model composition | ||
| Amino-acid residues‡ | A1–A43, A45–A89, A96–A210, B1–B90, B96–B210 | A1–A92, A99–A210, B1–B43, B46–B91, B97–B210, C1–C91, C94–C210, D1–D91, D96–D210 |
| Protein atoms | 3248 | 6481 |
| Mn3+ ions | 2 | 4 |
| Water molecules | 366 | 567 |
| Refinement details | ||
| R/Rfree (%) | 16.8 (20.9)/23.6 (26.6) | 17.4 (18.4)/22.3 (23.1) |
| No. of reflections | 19552/996 | 45781/2483 |
| 〈B〉 (Å2) | 25.3 | 22.1 |
| E.s.u. (based on Rfree) (Å) | 0.23 | 0.19 |
| R.m.s. deviations from ideal geometry | ||
| Bond lengths (Å) | 0.012 | 0.012 |
| Bond angles (°) | 1.30 | 1.23 |
| Ramachandran plot | ||
| Favoured regions (%) | 94.8/93.9 | 96.1/92.6/93.9/94.0 |
| Allowed regions (%) | 3.4/5.0 | 2.8/6.3/3.9/4.0 |
| Generously allowed regions (%) | 1.7/1.1 | 1.1/1.1/1.7/1.1 |
| Disallowed regions (%) | 0.0/0.0 | 0.0/0.0/0.6 (Cys96)/0.0 |
†
For crystal form II the completeness in the resolution range 41.2–2.25 Å is 95.4%.
‡
Some side chains are disordered and are not included in the final model. For crystal form I residues A126, B66 and B120 are truncated at Cδ, residues A40, A104, B40 and B43 are truncated at Cγ and residues A142 and B142 are truncated at Cβ. For crystal form II residues A142, A210, A53, A102, B40, B46, B53, B105, C91, C210, D139 and D158 are truncated at Cβ, while residues B23 and C94 are truncated at Sδ and Cγ, respectively.