Table 2. Quality statistics for SAD phasing using SeMet MmBag2(21103) and initial model building.

SAD phasing and model building
No. of Se atoms in protein	5
No. of protein copies in asymmetric unit	2
No. of placed Se atoms	8
Figure of merit	0.373
No. of residues built†	98
Bayesian map correlation coefficient‡	0.72
Final No. of residues built and refined§	138
Final R work/R free	0.319/0.363
Molecular-replacement statistics¶
No. of protein copies in asymmetric unit	8
Translation-function Z score (TFZ)	29.2
No. of C clashes (PAK)	0
Log-likelihood gain (LLG)	1469

^†Number of residues built by the PHENIX AutoBuild wizard out of 166 theoretically possible residues.

^‡Bayesian estimate of map quality determined by the PHENIX AutoSol wizard (Terwilliger et al., 2009 ▶).

^§Total number of residues, out of a theoretically possible 166 residues, built by a combined effort of automated building by PHENIX (Adams et al., 2010 ▶) followed by manual rebuilding in Coot (Emsley et al., 2010 ▶).

^¶Scores for the best Phaser (McCoy et al., 2007 ▶) molecular-replacement solution using the model built from the 3.1 resolution SAD data set.