TABLE 1.

Crystallographic data collection and refinement statistics

Structure	TPL-Ala	TPL-Met
Space group	P21212	P21212
Unit cell parameters
a (Å)	132.9	132.9
b (Å)	143.7	143.3
c (Å)	59.6	59.7
Resolution range (Å)	20.0–1.89 (1.93–1.89)a	30.0–1.95 (2.02–1.95)
No. of unique reflections	89 055 (4 337)	76 260 (6 854)
Rmerge (%)b	7.0 (35.7)	8.2 (42.5)
Average I/σ(I)	12.2 (1.8)	10.5 (2.3)
Data redundancyc	3.7 (2.3)	3.9 (3.6)
Completeness (%)	97.3 (87.5)	90.3 (82.3)
Wilson B-factor (Å2)	18.9	27.1
No. of reflections used in refinement	87 930 (4 337)	75 067 (7 386)
Rcryst (%)d	15.8 (23.2)	15.6 (19.2)
Rfree (%)d	19.8 (30.2)	19.2 (22.7)
No. of reflections used for Rfree	1 065 (52)	1 058 (116)
No. of protein residues	912	912
No. of water molecules	966	887
No. of ligands	6 (2 K+, 2 alanine quinonoid molecules, 2 PEG fragments)	6 (2 K+, 1 methionine quinonoid molecule, 1 PLP, 2 PEG fragments)
Average B-factor (Å2)
Chain A	17.2	32.0
Chain B	14.3	29.5
Water molecules	29.6	41.2
Overall	17.4	32.0
R.m.s. deviationse
Bond lengths (Å)	0.016 (0.022)	0.015 (0.022)
Bond angles (°)	1.4 (2.0)	1.4 (2.0)
Ramachandran plot (%)f
Favored	98.1	97.9
Outliers	0.0	0.0

^aValues in parentheses are for the outer resolution shell

^bThe value of the merging R-factor between equivalent measurements of the same reflection, R_merge = (Σ_hklΣ_i|<I_hkl> – I_{hkl, i}|)/(Σ_hklΣ_i I_{hkl, i})

^cThe average observation of the same reflection

^dCrystallographic R-factors, R = (Σ_hkl||F_{o, hkl}| – |F_{c, hkl}||)/(Σ_hkl F_{o, hkl}|)

^eTarget values are given in parentheses

^fAnalyzed by MolProbity (30)