Table 1. Crystallographic analysis of GFLV particles.
| Virus | GFLV-TD | GFLV-F13 |
| Data collection statistics £ | ||
| Beamline | ESRF/BM30 | SLS/X06DA |
| Space group (number) | P213 (198) | P1 (1) |
| Unit cell lengths a, b, c (Å) | 408.0 | 279.4 279.5 293.3 |
| Unit cell angles alpha, beta, gamma (°) | 90.0 | 102.4 116.4 108.2 |
| Resolution range (Å) | 36 – 2.7 | 135 – 3.0 |
| Highest resolution shell (Å) | 2.77 – 2.7 | 3.08 – 3.0 |
| No. of unique reflections | 563009 (32448) | 1214336 (73170) |
| Completeness (%) | 92.0 (72.0) | 88.1 (71.7) |
| Multiplicity | 11.0 (3.1) | 2.0 (1.9) |
| Rmerge (%)† | 12.5 (68.1) | 10.0 (35.0) |
| <I/sigma(I)> | 18 (1.9) | 9.2 (2.4) |
| Molecular replacement | ||
| Resolution range (Å) | 30 – 15 | 15 – 6.0 |
| Asymmetric unit content | 20-mer | 60-mer |
| Model | EM map | GFLV-TD |
| Correlation/R-factor(%)# | 60.4/56.4 | 70.6/34.7 |
| Refined atomic structure | ||
| Resolution range (Å) | 36 – 2.7 | 135 – 3.0 |
| R-factor/R-free (%)* | 19.3/21.0 | 19.0/20.7 |
| Number of capsid and solvent atoms | 79100/556 | 237060/– |
| Protein and solvent ADPs (Å2)** | 40.9/36.9 | 35.7/– |
| R.m.s.d. on bonds (Å) and angles (°) | 0.009/1.19 | 0.010/1.20 |
£: Statistics are given for reflections with I> = 0 and values in parentheses are for the highest resolution shell.
†Rmerge = σhkl σi |Ii(hkl) - <I(hkl)>|/σhkl σi Ii(hkl).
#
The high R-factor can be explained, among other reasons, by the model used (a low resolution EM reconstruction, without filtering) and the absence of a bulk solvent correction.
*The cross-validation (R-free) was calculated with 5% of the data.
**ADPs: Atomic displacement parameters.