Structural and Kinetic Characterization of Hyperthermophilic NADH-Dependent Persulfide Reductase from Archaeoglobus fulgidus
Table 1
X-ray data collection and refinement statistics for AfNpsr.
Data collection
Beamline
NE-CAT 24-ID-E
Wavelength (Å)
0.98
Space group
P1211
Unit cell dimensions (Å)
,, ,,
Resolution range (Å)
40-3.1 (3.27-3.10)
Total reflections
153,972 (22,435)
Unique reflections
41,638 (6083)
Completeness (%)a
99.7 (99.9)
CC 1/2
99.2 (76.1)
Multiplicity
5.2 (4.8)
()a
10.3 (2.6)
Rsymsym (%)a,b
11.9 (54.0)
Refinement
(%)c
19.0
(%)d
25.8
r.m.s. deviation bond length (Å)
0.021
r.m.s. deviation bond angles (°)
1.998
Dimers per ASU
2
No. protein atoms
16,267
No. nonprotein atoms
422
Water molecules
14
PDB code
6PFZ
aValues in parentheses are for the highest resolution shell. b, where is the th measured diffraction intensity and is the mean intensity for the Miller index ().c.d for a test set of reflections (5% in each case).
