Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3
Table 1
Data collection and refinement statistics of Phdpd.
Native
MAD (Se)
Data collection and phasing
Wavelength (Å)
1.0000
0.97929, 0.97950, 1.0000
Temperature (K)
100
100
Space group
212121
212121
Unit cell dimensions
a (Å)
57.9
57.8
b (Å)
88.8
88.8
c (Å)
147.6
147.1
(Å3 Da-1)
2.4
2.3
No. of molecules in asu
2
2
Resolution (Å)
2.4 (2.5-2.4)
2.3 (2.38–2.3)
No. of observations
182 560
192 019, 190 610, 177 795
No. of unique reflections
29 349 (2954)
34 548, 34 494, 33 486
Completeness (%)
95.9 (98.6)
99.3 (99.9), 99.2 (99.9), 96.5 (98.4)
11.2 (37)
7.0 (34.4), 5.7 (30.9), 5.2 (28.7)
—
0.45/0.57
Refinement
Resolution range (Å)
20.0–2.4
21.0
26.5
No. of protein atoms
5664
No. of solvent atoms
310
Ramachandran (%) in most favored
93.8
Allowed
5.7
Generously
0.5
PDB code
2HOW
, where is the observed intensity and is the average intensity from observations of symmetry related reflections, respectively. FOM, figure of merit. , where and are the observed and calculated structure factors, respectively. is the factor for a subset of 5% of the reflections that were omitted from refinement. As calculated by PROCHECK [23]. The values within the parentheses refer to the last shell.
