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Table 1 Crystallographic data and refinement statistics for the EphA4 structures

From: Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations

Data collection Crytal1 Crystal2
   Wavelength (Å) 1.5418 1.5418
   Resolution limit (Å) 50-2.9 50-2.4
   Space group P1 P1
Cell parameters   
   a, b, c (Å) 53.212, 70.621, 126.985 46.881, 70.030, 123.103
α, β, γ (°) 90.011, 90.036, 89.999 89.982, 89.972, 89.990
   Unique reflections 75555 98655
   Completeness 97.7% 94.6
   Redundancy 1.9 1.8
   Linear R-factor 0.473 0.094
Refinement   
   Resolution range (Å) 25.0-3.0 25.0-2.6
   R work 0.236 0.237
   Number of Reflections/test 34290/1816 48082/4071
   Rfree 0.312 0.262
   Rmsd bond lengths (Å) 0.013 0.011
   Rmsd bond angles (deg) 1.613 2.063
Ramachandran plot   
   Favored, % 75.9 72.9
   Allowed, % 18.2 21.4
   Generously allowed, % 3.5 3.2
   Disallowed, % 2.4 2.4