. Author manuscript; available in PMC: 2011 Jun 22.

Published in final edited form as: Biochemistry. 2010 Jun 22;49(24):5048–5056. doi: 10.1021/bi1005046

Table 2.

Anomalous scattering data collection statistics

Structure	D101L Co²⁺-HDAC8-M334 complex	D101L Fe²⁺-HDAC8-M334 complex	D101L Mn²⁺-HDAC8-M334 complex
Resolution limits, Å	50 – 2.7	50 – 3.0	35 – 2.7
Energy/wavelength (eV/Å)	7725/1.6050	7120/1.7143	8048/1.5406
Space Group	P2₁2₁2	P2₁2₁2	P2₁2₁2₁
Total/unique reflections	21,310/11,556	19,561/10,633	42,388/22,990
Completeness (%) (overall/outer shell)	99.9/100.0	98.5/89.1	95.7/97.8
Redundancy (overall/outer shell)	8.4/8.3	8.2/4.8	6.5/6.4
R_merge^a (overall/outer shell)	0.162/0.567	0.129/0.230	0.126/0.461
I/σ(I) (overall/outer shell)	13.0/5.2	15.7/4.8	11.2/4.4

R_merge = Σ|I−〈I〉|/Σ|I|, where I is the observed intensity and 〈I〉 is the average intensity calculated for replicate data.

Crystallographic R factor, R = Σ||F_o|−|F_c||/Σ|F_o|, for reflections contained in the working set. Free R factor, R_free = Σ||F_o|−|F_c||/Σ|F_o|, for reflections contained in the test set excluded from refinement. |F_o| and |F_c| are the observed and calculated structure factor amplitudes, respectively.