. Author manuscript; available in PMC: 2015 Jan 9.

Published in final edited form as: J Mol Biol. 2013 Sep 17;426(1):10.1016/j.jmb.2013.09.012. doi: 10.1016/j.jmb.2013.09.012

Table 2.

Crystal and X-ray data collection and crystallographic refinement statistics for the 14-3-3γ:THp-(1-43) complex which resulted in structural information for a dimeric 14-3-3γ and THp-(14-26) and THp-(11-22) fragments, each bound to a 14-3-3γ monomer.

Crystal data
Space group	P2₁2₁2₁
Cell dimensions
a, b, c (Å)	84.19, 115.12, 136.90
α=β=γ (°)	90.0
Data collection
Processing software	XDS
Wavelength (Å)	1.0331
Resolution (Å)	40.0-3.08 (3.16-3.08)
R_merge (%)	11.1 (49.2)
I / σI	11.6 (3.3)
Completeness (%)	87.1 (90.0)
No. of unique reflections	22015
Redundancy	5.1 (5.1)
Refinement
Processing software	Refmac 5
Resolution (Å)	3.08(3.16-3.08)
Reflections	20915(1565)
R_work / R_free (%)	21.0(28.1)/25.4(36.4)
No. atoms	7970
14-3-3gamma protein	7690
THp peptide fragment	280
Average B overall (Å²)	69.7
14-3-3gamma protein	69.0
THp peptide fragment	86.2
R.m.s.d. bond length (Å)	0.009
R.m.s.d. bond angle (°)	1.192
PDB entry	4J6S