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Table 1 Data collection and refinement statistics

From: Crystal structural analysis of human serum albumin complexed with hemin and fatty acid

DATA COLLECTION  
a (Å) 80.08
b (Å) 202.70
c (Å) 39.37
Resolution range (Å) 27.2–3.2
Independent reflections 10,825
Multiplicity 1 2.7(2.6)
Completeness (%) 96.2(92.4)
I/σ 8.1(2.1)
R merge (%) 2 5.7(34.5)
MODEL REFINEMENT  
Nonhydrogen atoms 4479
R model (%) 3 28.8
R free (%) 4 23.1
r.m.s deviation from ideal bond lengths (Å) 0.007
r.m.s deviation from ideal angles (°) 1.4
Average B-factor (Å 2 ) 75.3
PBD ID 1o9x
  1. 1Values for the outermost resolution shell are given in parentheses. 2 Rmerge = 100 × ∑ h j |I hj - I h |/∑ h j I hj where I h is the weighted mean intensity of the symmetry related reflections I hj 3 Rmodel = 100 × ∑ hkl |F obs - F calc |/∑ hkl F obs where I h where F obs and F calc are the observed and calculated structure factors respectively. 4R free is the R model calculated using a randomly selected 5% sample of reflection data omitted from the refinement.