TABLE 1.
Data collection, phasing, and refinement statistics for the spectrin B14–16 structure Data for the outermost shell are given in parentheses. r.m.s.d., root mean square deviation.
| Data collection | |||
| Crystal | Native | SeMeta | |
| Energy (eV) | 12,661.7 | 12,660 | |
| Resolution range (Å) | 43.60–1.95 (1.97–1.95) | 47.9–2.40 (2.42–2.40) | |
| Unique reflections | 55,069 (1,174) | 29,026 (438) | |
| Multiplicity | 4.2 (3.4) | 6.0 (2.2) | |
| Data completeness (%) | 97.3 (86.1) | 93.4 (57.5) | |
| Rmerge (%)b | 4.6 (68.2) | 7.6 (25.5) | |
| I/σ(I) | 29.4 (1.97) | 33.8 (3.47) | |
| Wilson B-value (Å2) | 30.2 | 42.7 | |
| Phase determination | |||
| Anomalous scatter | Selenium, 18 out of 18 possible sites | ||
|
Figure of merit (30-2.40 Å)
|
0.18 (0.67 after density modification)
|
||
| Refinement statistics | |||
| Resolution range (Å) | 28.6–1.95 (1.98–1.95) | ||
| No. of reflections (Rwork/Rfree) | 52,170/2788 (2241/111) | ||
| Data completeness (%) | 97.2 (85.0) | ||
| Atoms (non-H protein/solvent/other) | 5479/561/33 | ||
| Rwork (%) | 19.2 (24.0) | ||
| Rfree (%) | 25.0 (32.9) | ||
| r.m.s.d. bond length (Å) | 0.008 | ||
| r.m.s.d. bond angle | 0.845° | ||
| Mean B-value (Å; protein/solvent/other) | 39.6/44.8/64.4 | ||
| Ramachandran plot (%; favored/additional/disallowed)c | 99.7/0.3/0.0 | ||
| Maximum likelihood coordinate error | 0.31 | ||
| Missing residues | Chain A, none; chain B, Leu2015 | ||
| Alternate conformations | Chain A, 8; chain B, 8 | ||
a
Bijvoet pairs were kept separate for data processing
b
Rmerge = 100 ΣhΣi|Ih,i – 〈Ih〉|/ΣhΣhIh,i, where the outer sum (h) is over the unique reflections, and the inner sum (i) is over the set of independent observations of each unique reflection
c
This was as defined by the validation suite MolProbity (17)