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. Author manuscript; available in PMC: 2014 May 27.
Published in final edited form as: J Mol Biol. 2013 Feb 19;425(10):1731–1744. doi: 10.1016/j.jmb.2013.02.012

Table 1. X-ray data and refinement statistics.

gp15 C-terminal truncation mutant (residues 1–261)

Full length gp15 Triclinic, Pt derivative


Trigonal, native Trigonal, native Peak Inflection point
X-ray wavelength (Å) 1.0 0.97941 1.07195 1.07228
Space group P32 P1 P1
Cell dimensions
a, b, c (Å) 100.68, 100.68, 155.891 65.87, 76.31, 93.89 65.89, 77.01, 94.16
 α, β, γ (°) 90, 90, 120 109.04, 104.62, 89.30 109.01, 104.43, 88.94
Resolutiona (Å) 2.7 (2.75–2.7) 3.2 (3.31–3.2) 3.6 (3.73–3.6) 3.6 (3.73–3.6)
Rmergea 0.078 (0.27) 0.077 (0.21) 0.076 (0.17) 0.073 (0.27)
I/σa 20.0 (3.3) 18.7 (5.9) 15.9 (5.6) 17.3 (3.6)
Completenessa (%) 93 (85) 92 (72) 79 (58) 77(51)
Redundancya 5.5 (2.3) 3.8 (3.5) 2.3 (2.2) 2.3 (2.1)

Refinement statistics

Crystal form Trigonal, native Triclinic, native
Resolution (Å) 2.7 3.2
No. of reflections 45,176 25,229
No. of atoms
 Protein 10,452 10,145
 Water 72 0
Rwork/Rfree 0.207/0.252 0.171/0.202
Root-mean-square deviations
 Bond length (Å) 0.010 0.009
 Bond angles (°) 1.30 1.22
 Average B-factor (Å2) 64 62
Ramachandran plot (%)
 Favored 90 90
 Outliers 1.9 2.0
a

Numbers in parentheses represent values in the highest-resolution shell.