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. Author manuscript; available in PMC: 2010 Apr 1.
Published in final edited form as: Proteins. 2009 Apr;75(1):217–230. doi: 10.1002/prot.22236

Table V.

Crystallographic statistics for the refinement of perch Hb at pH 5.7, 6.3, and 8.0. Statistics listed in parentheses are for those in reported in the last refinement shell listed in the resolution range.

Perch Hb
pH 5.7 pH 6.3 pH 8.0
Data Collection
 Resolution range (Å) 69.67–1.90
(1.95–1.90)
70.01–2.00
(2.05–2.0)
69.50–2.10
(2.16–2.10)
 Space Group P212121 P212121 P212121
 Unit cell dimensions
 a × b × c (Å)
57.2 × 84.8 ×
121.9
α=β=γ=90°
57.6 × 85.0 ×
123.2
α=β=γ=90°
57.7 × 84.9 ×
121.5
α=β=γ=90°
 Unique reflections 46,999 42,699 37,394
 Completeness (%) 98.7 (84.5) 96.3 (69.9) 97.4 (86.8)
 Average I/σI 14.5 (3.1) 16.2 (2.9) 12.8 (3.3)
 Redundancy 8.3 (4.1) 9.2 (4.0) 5.9 (4.3)
 Ligand State Met Met Met
Refinement Statistics
 Rwork 18.5 (22.9) 18.4 (21.9) 20.4 (24.6)
 Rfree 23.0 (27.7) 23.2 (31.1) 25.2 (30.2)
 Average B-value (Å2) 17.6 23.0 29.8
 Protein B-value (Å2) 15.1 21.6 28.6
 Water B-value (Å2) 42.1 40.5 48.7
 Heme B-value (Å2) 33.3 33.1 42.4
 No. of atoms in assym.
unit
4974 4950 4828
 Rmsd bond length (Å) 0.017 0.021 0.014
 Coordinate error
 (maximum likelihood,
Å)
0.11 0.13 0.18
Ramachandran plot,
residues
 In most favored regions
(%)
93.7 92.2 91.8
 In allowed regions (%) 6.3 7.8 8.2
PDB ID 3BJ1 3BJ2 3BJ3