TABLE 1.
Crystal parameters, x-ray data collection, phasing, and refinement statistics
| Peak | |
|---|---|
| Space group | P21 |
| Unit cell parameters (Å, °) | a = 63.6, b = 32.8, c = 114.4, β = 105.2 |
| Data collection statistics | |
| Wavelength (Å) | 0.97934 |
| Energy (eV) | 12,660 |
| Resolution range (Å) | 44.75–3.00 (3.11–3.00) |
| No. of reflections (measured/unique)a | 61747/9770 |
| Completeness (%) | 96.7 (79.8) |
| Rmergeb | 0.086 (0.342) |
| Redundancy | 6.3 (4.3) |
| Mean I/sigma(I) | 10.0 (3.0) |
| Phasing statisticsc | |
| Phasing power (isomorphous/anomalous) | 0.0/1.37 |
| Mean FOM (centric/acentric) | 0.09/0.285 |
| Rcullis (isomorphous/anomalous) | 0.0/0.736 |
| Refinement and model statistics | |
| Resolution range | 44.75–3.00 (2.15–2.10) |
| No. of reflections (total/test) | 9242/753 |
| Rcrystd | 0.236 (0.264) |
| Rfreee | 0.288 (0.386) |
| Root mean square deviation bonds (Å) | 0.008 |
| Root mean square deviation angles (°) | 1.047 |
| ESU from Rfree (Å) | 0.542 |
| TLS groups (residue range) | A39–A70, A71–A147, A148–A158, A159–A235 B40–B70, B71–B143, B158–B234 |
| B factor - Wilson (Å2) | 75.5 |
| Average B factor – molecule A/B (Å2) | 72.4/72.8 |
| No. of protein molecules/all atoms | 2/3103 |
| No. of waters/zinc(II)/sulfates | 0/2/1 |
| Ramachandran Plot by MOLPROBITY (%) | |
| Favored regions | 95.1 |
| Additional allowed regions | 4.6 |
| Outliers | 0.3 (Asp-A54) |
| Protein Data Bank code | 3bvo |
a
The values in parentheses are for the highest resolution shell
b
Rmerge = ΣhΣi|Ii(h) – 〈I(h)〉|/ΣhΣiIi(h), where Ii(h) is the intensity of an individual measurement of the reflection, and 〈I(h)〉 is the mean intensity of the reflection
c
Phasing by SHARP in 36.78–3.00 Å resolution range
d
Rcryst = Σh|Fobs| – |Fcalc|/Σh|Fobs|, where Fobs and Fcalc are the observed and calculated structure-factor amplitudes, respectively
e
Rfree was calculated as Rcryst using ∼8.1% of the randomly selected unique reflections that were omitted from structure refinement