Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity

Table 1 Crystallographic statistics.

Resolution range (Å)	19.73 - 1.94
Unit cell dimensions a,b,c (Å) β (°)	76.6, 43.6, 71.7, 98.3
Space group	C 2
No. reflections measured, unique	71,206, 17.242
Multiplicity^a , Completeness (%)	4.1(3.3), 98.9 (93.3)
Wilson B (Å²)	24.5
R_merge(%)^b , < I/?(I) >	5.3 (37.3), 17.5 (3.2)
Protein residues, water molecules	266, 185
R_work(%)^c , R_free(%)^d	18.3, 24.1
DPI (Å)^e	0.18
Average B-factors (Å²)
Overall, main chain, side chain, waters	30.6, 29.3, 31.8, 31.3
R.m.s.d bond lengths (Å), angles (°)	0.012, 1.25
Ramachandran plot analysis (%)
Favorable, Outliers	97.7, 0

^a.Values in parentheses refer to the highest resolution shell. 2.05 - 1.94 Å ^b.R_merge= ∑_hkl∑_i| I_i(hkl) - < I(hkl)>|/ ∑_hkl∑_iI_i(hkl); where I_i(hkl) is the intensity of the i th measurement of reflection hkl and < I(hkl)> is the mean value of I_i(hkl) for all i measurements. ^c.R_work= ∑_hkl||F_o|-|F_c||/∑|F_o|, where F_ois the observed structure factor and F_cis the calculated structure factor. ^d.R_freeis the same as R_crystexcept calculated with a subset, 5%, of data that are excluded from refinement calculations.^e.DPI, Diffraction-component Precision Index [39].

ISSN: 1472-6807