Crystal Structure of PAV1-137: A Protein from the Virus PAV1 That Infects Pyrococcus abyssi

Table 1

Data collection and refinement statistics.

Data collection
Space group	P6122
Cell dimensions a, b, c (Å)	73.55, 73.55, 191.55
Wavelength (Å)	0.9793
Resolution (Å)	20.0–2.20
Outer resolution shell (Å)	2.32–2.20
Number of observed reflections/unique	94031/15911
Completeness (%) (outer shell)	97.4 (85.3)
Multiplicity (outer shell)	5.9 (2.8)
𝐼/𝜎(𝐼) (outer shell)	19.0 (2.4)
𝑅merge (%)^1 (outer shell)	5.8 (45.9)
Refinement
Resolution (Å)	20.0–2.20
Reflections (working/test)	15873/800
𝑅/𝑅free (%)^2	21.5/24.7
RMSD
Bond lengths (Å)	0.010
Bond angles (°)	1.15
B-factors (Å^2)
Protein	63
Ramachandran statistics (%)
Most favored	98.71
Allowed	1.29

¹𝑅_merge=∑_ℎ∑_𝑖|𝐼_ℎ𝑖−⟨𝐼_ℎ⟩|/∑_ℎ∑_𝑖𝐼_ℎ𝑖, were 𝐼_ℎ𝑖 is the ith observation of the reflection h, while ⟨𝐼_ℎ⟩ is the mean intensity of reflection h.
²𝑅=∑||𝐹_𝑜|−|𝐹_𝑐||/|𝐹_𝑜|. 𝑅_free: was calculated with a set of randomly selected reflections (5%).