Table 1.

Statistics of crystallographic analysis

Data collection
Crystal	hPDILT
Wavelength (Å)	0.979
Space group	P32
Cell dimensions
a, b, c (Å)	97.4, 97.4, 57.6
α, β, γ (°)	90.0, 90.0, 120.0
Resolution range (Å)	50.00–2.38 (2.42–2.38)a
Rsym	0.066 (0.716)
Completeness (%)	99.8 (100.0)
Redundancy	3.8 (3.8)
I/σ(I)	20.6 (2.0)
Refinement
Resolution (Å)	28.10–2.38
No. of reflections	24393
Rwork /Rfree (%)	19.7/23.5
No. of atoms
Protein/water	3764/80
B-Factors (Å2)
Protein/water	56.0/49.6
Root mean square deviations
Bond lengths (Å)	0.008
Bond angles (°)	0.957
Ramachandran statistics (%)b
Most favored regions	97.6
Additional allowed regions	2.4
Disallowed regions	0.0
Side chain outliers	0.0
Clashscore	0.0

^a Highest resolution shell is shown in parentheses.

^b Data were as defined by the validation suite MolProbity.