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

BMC Structural Biology

Table 1 Data collection and refinement statistics

*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

¹Values for the outermost resolution shell are given in parentheses. ² R_merge = 100 × ∑_h∑_j|I_hj- I_h|/∑_h∑_jI_hjwhere I_his the weighted mean intensity of the symmetry related reflections I_hj³ R_model = 100 × ∑_hkl|F_obs- F_calc|/∑_hklF_obswhere I_hwhere F_obsand F_calcare the observed and calculated structure factors respectively. ⁴R_freeis the R_modelcalculated using a randomly selected 5% sample of reflection data omitted from the refinement.

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