Table 1.

Structure Determination

Diffraction Data StatisticsAvrL567-AAvrL567-D
Resolution (Å)50.0–1.43 (1.468–1.432)a50.0–2.26 (2.316–2.262)a
Observations337,806102,320
Unique reflections28,1497,619
Completeness (%)99.1 (93.3)99.7 (98.5)
Rmerge (%)b0.056 (0.238)0.113 (0.497)
Average I/σ(I)33.7 (13.95)11.9 (8.35)
Refinement statistics
    Resolution (Å)42.1–1.43 (1.468–1.432)40.26–2.26 (2.316–2.262)
    Number of reflections26,4367,199
    Rcrystc0.220 (0.387)0.195 (0.240)
    Rfreed0.254 (0.384)0.257 (0.352)
Number of nonhydrogen atoms:
    Protein1104913
    Solvent199103
    Mean B-factor (Å2)24.628.4
    Coordinate error (Å)0.1980.250
Root mean square deviations from ideal values:
    Bond lengths (Å)0.0150.019
    Bond angles (°)1.6171.702
Ramachandran plot:
    Residues in most favored (disallowed) regions (%)e88.9 (0)87.9 (0)
  • a Numbers in parenthesis are for the highest resolution shell.

  • b Rmerge = ∑hkl(∑i(|I hkl,i − <I hkl >|))/∑hkl,i <I hkl>, where I hkl,i is the intensity of an individual measurement of the reflection with Miller indices h, k, and l, and <Ihkl> is the mean intensity of that reflection. Calculated for I > −3σ(I).

  • c Rcryst = ∑hkl(‖Fobshkl| − |Fcalchkl‖)/|Fobshkl|, where |Fobshkl| and |Fcalchkl| are the observed and calculated structure factor amplitudes.

  • d Rfree is equivalent to Rcryst but calculated with reflections (5%) omitted from the refinement process.

  • e Calculated with the program PROCHECK (Laskowski et al., 1993).

  • fCalculated based on the Luzzati plot with the program SFCHECK (Vaguine et al., 1999).