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Table 1 Data collection and refinement statistics

From: Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus

Data collection

 

   Data set

ESRF ID29

   Wavelength (Å)

1.0088

   Resolution (Å)

15.0–3.3 (3.42–3.3)

   Completeness (%)

99.4 (100.0)

   Total reflections

59756

   Unique reflections

9304

   1Rmerge

0.074 (0.375)

   <I>/<σI>

14.8 (4.6)

   Space group

P 43212

   Lattice parameters (Å)

a, b = 73.056; c = 224.434

   Molecules / a.u.

2

   Matthews coefficent

3.74

   Solvent content (%)

66.9

Refinement

 

   Resolution range (Å)

14.97 – 3.34

   Number of reflections / test set

9251 / 500

   2Rfactor

0.3088

   Rfree

0.3754

   Residues

227 (out of 360)

   Number of protein atoms

1622

   Average B factor (Å2)

42.34

Model geometry

 

   Bond length r.m.s.d from ideal (Å)

0.016

   Bond angle r.m.s.d. from ideal (°)

1.610

Ramachandran plot3

 

   % in most favoured regions

81.8

   % in additionally allowed regions

16.8

   % in generously allowed regions

1.4

  1. Values in parenthesis are for last shell limits. 1Rmerge = Σhkl Σi |Ii (hkl) - <I(hkl)>| / Σhkl Σi Ii (hkl) 2Rfactor = Σhkl ||Fobs| - k |Fcalc|| / Σhkl |Fobs| 3As defined in PROCHECK [56]