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. Author manuscript; available in PMC: 2009 Aug 3.
Published in final edited form as: Biochemistry. 2009 Jun 16;48(23):5210–5217. doi: 10.1021/bi9001216

Table 2.

Crystallographic data collection and refinement parameters

PFA1-
Ror2(518–525)
PFA1-PYRO-
Glu3-Aβ(3–8)
Data collection
Space group P1 P1
Cell dimensions
   a, b, c (Å) 41.6 41.7
42.6 42.7
58.7 58.6
   α, β, γ (°) 96.1 96.1
93.6 93.8
91.7 91.7
Resolution (Å) 30-2.7 35-1.9
(last shell) (2.8-2.7) (2.02-1.95)
Rsym 0.083(0.222) 0.049(0.284)
I / σI 12.8(2.8) 17.5(2.2)
Completeness 85.0(49.9) 86.4(54.2)
(%)
Redundancy 2.3(1.6) 1.8(1.5)
Refinement
Resolution (Å) 2.7 1.9
No. reflections 8780 23906
TLS groups 5 0
Rwork / Rfree % 17.7/24.8 20.4/25.6
No. atoms
   Protein(non-H) 3421 3495
   Ligand/ion 0 6 (glycerol)
   Water 23 113
B-factors (Å2) 32 35
   Bound peptide 40 52
   Ligand/ion None 41 (glycerol)
   Water 30 40
R.m.s deviations
Bond lengths (Å) 0.010 0.010
Bond angles (°) 1.2 1.3
Ramachandran 99.5% 99.7%
allowed region
PDB code 3EYU 3EYS