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. 2006 Sep 30;62(Pt 10):1021–1023. doi: 10.1107/S1744309106036232

Table 1. Diffraction data statistics of four crystal forms of the Atg5–Atg16 complex.

Values in parentheses refer to the outer shell.

Crystal form I II III IV
Protein complex Atg5–Atg16(1–46) Atg5–Atg16(1–57) Atg5–Atg16(1–57) Atg5–Atg16(1–57)
Space group P21 P21 P21 P42212
Unit-cell parameters        
a (Å) 66.3 79.5 56.9 73.3
b (Å) 104.4 101.4 101.2 73.3
c (Å) 112.2 95.1 66.5 148.1
 β (°) 92.1 98.6 100.6 90
Resolution range (Å) 50–2.1 (2.18–2.10) 50–2.95 (3.06–2.95) 50–3.0 (3.11–3.00) 50–1.97 (2.04–1.97)
Observed reflections 317606 169957 74216 257319
Unique reflections 88015 31125 14118 29390
Completeness (%) 98.6 (95.7) 98.8 (91.5) 94.3 (77.8) 99.9 (100.0)
Rmerge(I) 0.048 (0.306) 0.092 (0.312) 0.090 (0.304) 0.055 (0.304)
I/σ(I) 15.0 (3.8) 8.7 (3.9) 10.9 (4.0) 28.9 (11.1)

R merge(I) = Inline graphic Inline graphic, where I i is the intensity of the ith observation and 〈I〉 is the mean intensity.