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. 2008 Nov 21;283(47):32831–32838. doi: 10.1074/jbc.M801266200

TABLE 1.

Crystallographic data and refinement statistics

Data collection Native (collected at 100 K)
Resolution (Å) 33.02-2.48 (2.59-2.48)
Crystallographic cell - P1 a = 63.6 Å, b = 71.4 Å, c = 100.2 Å, α = 98.5°, β = 90.6°, γ = 90.1°
Observations 255,677
Unique reflections 61,295
Completeness (%) 98.6 (98.3)
Redundancy 4.2 (3.6)
Rmerge (%) 8.5 (44.8)
<II> 15.0 (2.3)
Wilson plot B factor (Å2) 48.8
Model refinement
Reflections (total/free) 61,224/3,144
Rfactor (Rfree), (%) 22.6 (27.8)
Atoms (total/protein) 9,730/9,508
Root mean square deviation from ideal
Bonds (Å) 0.010
Angles (°) 1.26
<B> factors, all atoms (Å2) 45.3
Complex 1
Activin A (chain A/chain B) 33.3/32.8
FSTL3 (chain C/chain D) 48.1/41.1
Complex 2
Activin A (chain E/chain F) 32.6/32.9
ESTL3 (chain G/chain H) 48.1/41.0
Other molecules (number, <B> factor)
Water 214 (45.6)
Sulfate 1 (80.0)
N-acetylglucosamine 2 (74.1)
Ethylene glycol 3 (65.4)
Ramachandran plot statistics (number)
Most favored 90.5% (963)
Additionally allowed 8.6% (92)
Generously allowed 0.5% (5)
Disallowed 0.4% (4) (Asn38 in all activin A chains)