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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