Table 1. Crystallographic data collection and refinement statistics.
SAYabJ | |
---|---|
Data collection | |
Beamline | PAL-5C |
Wavelength (Å) | 0.98 |
Resolution range1 (Å) | 40.00–1.75 (1.78–1.75) |
Space group | P21 |
Unit cell parameters (Å) | a = 47.12 |
b = 83.22 | |
c = 89.36 | |
Observations (total/unique) | 277503/133402 |
Completeness (%) | 97.4 (95.1) |
CC1/2 | 0.98 (0.92) |
Rsym2 | 5.6 (20.4) |
I/sigma | 42.6 (6.9) |
Refinement | |
Rwork3 (%) | 17.4 |
Rfree3 (%) | 21.2 |
Protein atoms | 5838 |
Water molecules | 499 |
Average B value (Å2) | 25.0 |
r.m.s.d. bond (Å) | 0.006 |
r.m.s.d. angle (°) | 0.801 |
Ramachandran analysis (%) | |
Favored region | 95.6 |
Allowed region | 4.4 |
Outliers | 0.0 |
Numbers in parentheses indicate the statistics for the last resolution shell.
, where Ihkl = single value of measured intensity of hkl reflection, and <Ihkl> = mean of all measured value intensity of hkl reflection.
, where Fobs = observed structure factor amplitude, and Fcalc = structure factor calculated from model. Rfree is computed in the same manner as Rwork, but from a test set containing 5% of data excluded from the refinement calculation.