Table 2.
Summary of Crystallographic Analysis
| Diffraction Data |
|||||||
|---|---|---|---|---|---|---|---|
| Data Set | λ (Å) | Resolution (Å) | Number of Reflections (Total/Unique) | Completeness (%) | I/σ(I) | Rsyma (%) | Phasing Power (Ano/Iso) |
| C44 | |||||||
| Native | 1.0055 | 45.2–1.70 | 66,857 (9,539)b | 99.9 (100) | 16.5 (5.7) | 6.3 (38.2) | |
| NaBr λ1 | 0.9203 | 50–2.0 | 45,596 (1,0619) | 97.9 (99.3) | 18.8 (8.0) | 6.4 (19.1) | 0.4/0.5 |
| NaBr λ2 | 0.9200 | 50–2.0 | 45,719 (10,700) | 97.9 (99.3) | 16.1 (6.8) | 7.1 (24.9) | 0.7/0.2 |
| NaBr λ3 | 0.9070 | 50–2.0 | 44,184 (10,689) | 97.6 (98.2) | 15.6 (5.7) | 7.8 (31.8) | 0.5/– |
| N50/C36 | |||||||
| 0.9788 | 70.7–1.95 | 81,203 (32,684) | 94.5 (94.8) | 11.1 (3.1) | 5.5 (38.7) | ||
| N37(L6)C34 | |||||||
| 1.0358 | 72.6–1.50 | 69,620 (11,906) | 98.0 (99.2) | 15.6 (7.1) | 5.8 (25.5) | ||
| N34 | |||||||
| 0.9788 | 51.6–1.70 | 33,119 (11,231) | 96.9 (94.7) | 21.1 (5.1) | 3.6 (21.0) | ||
| Refinements | C44 | N50/C36 | N37(L6)C34 | N34 |
|---|---|---|---|---|
| Resolution (Å) | 45.2–1.70 | 70.7–1.95 | 72.6–1.50 | 51.6–1.70 |
| Number of reflections | 9,076 | 31,031 | 11,341 | 10,695 |
| Number of protein atoms | 551 | 3,668 | 551 | 763 |
| Number of water molecules | 73 | 176 | 77 | 100 |
| Rcryst/Rfree (%)c | 20.9/25.8 | 20.3/27.4 | 21.1/24.6 | 19.4/23.8 |
| Rmsd bond lengths (Å) | 0.015 | 0.033 | 0.013 | 0.014 |
| Rmsd bond angles (°) | 1.6 | 2.3 | 1.4 | 1.3 |
| Average B factor (Å2) | 15.9 | 17.1 | 11.9 | 18.2 |
| Rmsd B values (Å2) | 1.9 | 4.7 | 1.3 | 2.1 |
a
Rsym = Σ|I − <I>|/ΣI, where I is the integrated intensity of a given reflection.
b
Numbers in parentheses represent the statistics for the shell comprising the outer 10% (theoretical) of the data.
c
Rcryst = Σ|Fo − Fc|/ΣFo, Rfree = Rcryst calculated by using 5% of the reflection data chosen randomly and omitted from the start of refinement.