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. 2000 Aug 15;97(17):9413–9418. doi: 10.1073/pnas.97.17.9413

Table 2.

Statistics of the refinement of the atomic model of d-LDH to x-ray diffraction data

Resolution range 20 − 1.9, Å
Protein atoms   8,533
Solvent atoms 392
Unique reflections  76,528
Rwork*  20.1, %
Rfree  24.5, %
rms deviation bond lengths   0.024, Å
rms deviation bond angles   2.43°
rms deviation between NCS related molecules   0.32, Å
*

Rwork = Σ(h,k,l)Fo| − |Fc∥/Σ(h,k,l) |Fo|, where Fo and Fc are the observed and calculated structure factors, respectively. 

Rfree = Σ(h,k,l)ɛTFo| − |Fc∥/Σ(h,k,l)ɛT |Fc|, where T is the test set containing a randomly selected 10% of the observed reflections omitted from the refinement process.