Structure of Arabidopsis thaliana 5-methylthioribose kinase reveals a more occluded active site than its bacterial homolog

Table 1 Diffraction Data and Crystallographic Refinement Statistics

Space Group	C2
Cell dimensions (Å, °)	a = 162.5, b = 82.2, c = 91.1 β = 117.8
Wavelength (Å)	1.0
Resolution (Å)	80.6 – 1.9
Average redundancy^a	3.4 (2.9)
R_merge^b (%)^a	4.5 (17.5)
Completeness (%)^a	98.7 (90.8)
<I>/σI^a	16.9 (4.8)
Number of reflections (working/test)	78352/4105
Number of protein atoms/heteroatoms^c	6648/103
Number of water molecules	778
R_cryst/R_free (%)^d	16.3/19.7
RMS deviation from ideal values
Bond length (Å)	0.014
Bond angle (°)	1.4
Average B factor (Å²)
Proteins	16.4
Ligands (ADP and MTR)	16.4
Magnesium ions	18.0
Chloride ions	20.7
Water molecules	25.3
Ramachandran Plot^e
Total Favoured (%)	97.8
Total Allowed (%)	100
DPI^f coordinate error based on R_free (Å)	0.13

^aValues in parentheses corresponds to the value in highest resolution shell (1.97–1.90Å).
^bR_merge = ∑∑|I (k) - <I>|/∑I (k) where I (k) and <I> represent the diffraction intensity values of the individual measurements and the corresponding mean values. The summation is over all unique measurements.
^cHeteroatoms include ADP, MTR, ethylene glycol, magnesium and chloride ions.
^dR_cryst = ∑|F_obs - F_calc|/∑|Fobs|; R_free is R_cryst for the 5% cross validated test data.
^eAs defined by the Ramachandran plot in MolProbity [53].
^fCruickshank's diffraction component precision index (DPI) [54] as an estimate of coordinate error.

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