Table I.
Crystallographic statistics for data collected on native and selenomethionine Hel308
| Native | Se-Peak | |
|---|---|---|
| Data collection | ||
| Space Group | P21 | P21 |
| Unit Cell | a=61.7 | a=61.8 |
| b=138.1 | b=138.0 | |
| c=107.6 | c=107.5 | |
| β=94.7 | β=95.2 | |
| Resolution (Å) | 30-2.3 (2.42-2.3) | 30-2.6 (2.74-2.6) |
| Wavelength (Å) | 0.934 | 0.979 |
| Unique reflections | 79222 (11421) | 54876 (7481) |
| Multiplicity | 6.0 (3.6) | 3.7 (3.7) |
| Completeness (%) | 99.8 (99.3) | 99.5 (98.3) |
| Rmerge (%) | 7.8 (30.9) | 8.3 (35.8) |
| I/σ(I) | 14.7 (4.2) | 11.2 (4.3) |
| Structure solution | ||
| Monomers | 2 | 2 |
| Selenium sites | 24 | |
| Refinement | ||
| Protein atoms | 11116 | |
| Sulfate ions | 7 | |
| Waters | 146 | |
| Average B-factors (Å2) | ||
| Chain A | 45.76 | |
| Chain B | 45.92 | |
| Sulfate ions | 48.75 | |
| Waters | 39.58 | |
| Monomer superposition rmsd(Å) | ||
| Domains 1 to 5 | 0.874 (690 residues) | |
| Domains 1 to 4 | 0.446 (630 residues) | |
| Domain 5 | 0.389 (61 residues) | |
| r.m.s.d. bond lengths(Å) | 0.011 | |
| Angles (°) | 1.18 | |
| Rfactor/Rfree (%) | 21.2 (25.9) | |
| Validation | ||
| Ramachandran angles | ||
| Favored(#,%) | 97.5 | |
| Disallowed(#,%) | 0.07 |
#
Molprobity definition (26).