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Table 1 Data collection and refinement statistics

From: Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin

Space-group

P1

a, b, c (Å)

55.07, 55.44, 119.85

α, β, γ (°)

81.00, 90.83, 64.52

Resolution range (Å)

59-2.75

Independent reflections

31655

Multiplicity 1

1.9 (1.9)

Completeness (%)

95.5 (92.9)

I/σ I

8.2 (1.7)

R merge (%) 2

9.1 (34.5)

MODEL REFINEMENT

 

Nonhydrogen atoms

 

R model (%) 3

19.6

R free (%) 4

23.2

r.m.s bonds (Å)

0.009

r.m.s bond angles (°)

1.18

Average overall B-factor (Å 2 )

46.2

Average ligand B-factors (Å 2 ) 5

18.0, 36.2, 87.1, 111.9

Ramachandran plot (% favoured/allowed)

89.9/8.4

PDB ID

2ydf

  1. 1Values for the outermost resolution shell are given in parentheses.
  2. 2R merge = 100 × Σ h Σ j |I hj - I h |/ Σ h Σ j I hj where I h is the weighted mean intensity of the symmetry related reflections I hj
  3. 3R model = 100 × Σ hkl |F obs - F calc |/ Σ hkl F obs where F obs and F calc are the observed and calculated structure factors respectively.
  4. 4Rfree is the Rmodel calculated using a randomly selected 5% sample of reflection data omitted from the refinement.
  5. 5Average B-factors given for iophenoxic acid ligands bound to sub-domains IIA, IIIA, IB and in the IIIA-IIIB sites respectively.
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BMC Structural Biology

ISSN: 1472-6807

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