Table 1.
Data collection and refinement statistics for X-ray crystallography
| Data collection statisticsa | |||
| Resolution (Å) | 30–2.0 (2.05–2.00) | ||
| Completeness (%) | 91.7 (63.9) | ||
| Multiplicity | 2.7 (1.9) | ||
| I/σI | 20.2 (3.0) | ||
| Number of observations/unique reflections | 690,731/74,855 | ||
| Rsymb | 5.1 (25.9) | ||
| Refinement statistics | |||
| Wilson B/average B | 29.5/36.0 | ||
| Number of non-H atoms/waters | 6958/802 | ||
| Number of reflections | 70,789 (3611) | ||
| RMSDc bonds/angles | 0.014/1.5 | ||
| Ramachandrand | 89.2 9.6 0.5 0.7 | ||
| Rcryst/Rfreee (%) | 20.0/24.3 | ||
| B-factor (Å2) | B-factor of equivalent domain in JM22 (Å2) | RMSD with JM22 (% α-carbon residues used) | |
|---|---|---|---|
| 1F1E8hu | 35.8 | 34.4 | 2.1 (90) |
| 1F1E8hu Vα | 35.5 | 28.0 | 1.5 (96) |
| 1F1E8hu Vβ | 36.2 | 27.3 | 1.1 (98) |
| 1F1E8hu Cα | 36.4 | 52.5 | 2.3 (78) |
| 1F1E8hu Cβ | 35.4 | 37.0 | 0.6 (99) |
RMSDs were calculated using the program SHP (D. I. Stuart, unpublished).
a
Data in parenthesis are for the highest-resolution shell.
b
Rsym = σj|〈I〉 − Ij|/σ〈I〉 where Ij is the intensity of the jth reflection, and 〈I〉 is the average intensity.
c
Root-mean-square deviation from ideal values.
d
Values are expressed as the percentage of amino acids in the “core,” “allowed,” “generously allowed,” and “disallowed” regions, respectively.
e
Five percent of data have been set aside for cross-validation calculations.