Table 1. Summary of crystal parameters, data-collection and refinement statistics for YP_001813558.1 (PDB code 3nl9).

Values in parentheses are for the highest resolution shell.

	λ1 MADSe	λ2 MADSe
Crystal parameters
Space group	C2
Unit-cell parameters (Å, °)	a = 52.09, b = 69.04, c = 50.21, β = 111.8
Mosaicity (°)	0.91
Data collection
Wavelength (Å)	1.0000	0.9798
Resolution range (Å)	39.6–1.78 (1.83–1.78)	39.6–1.78 (1.83–1.78)
No. of observations	43073	43110
No. of unique reflections	15531	15528
Completeness (%)	98.1 (97.9)	98.1 (97.3)
Mean I/σ(I)	9.8 (2.1)	8.6 (1.8)
Rmerge on I†	0.069 (0.555)	0.082 (0.563)
Rmeas on I‡	0.086 (0.687)	0.102 (0.698)
Rp.i.m. on I§	0.050 (0.401)	0.059 (0.408)
Overall B factor from Wilson plot (Å2)	21.3	21.0
Model and refinement statistics
Data set used in refinement	λ1 MADSe
Resolution range (Å)	39.6–1.78
No. of reflections (total)	15531
No. of reflections (test)	788
Completeness (%)	97.8
Cutoff criterion	|F| > 0
Rcryst¶	0.177
Rfree††	0.222
Stereochemical parameters
Restraints (r.m.s.d. observed)
Bond angles (°)	1.30
Bond lengths (Å)	0.015
Average protein isotropic B value (Å2)	26.0‡‡
Average solvent isotropic B value (Å2)	33.6
ESU§§ based on Rfree (Å)	0.14
Protein residues/atoms	169/1340
Water/cryoprotectant molecules	141/2

^† R _merge = .

^‡The redundancy-independent (multiplicity-weighted) merging R factor, R _meas = (Diederichs & Karplus, 1997 ▶).

^§The precision-indicating merging R factor, R _p.i.m. = (Weiss & Hilgenfeld, 1997 ▶; Weiss et al., 1998 ▶).

^¶ R _cryst = , where F _calc and F _obs are the calculated and observed structure-factor amplitudes, respectively,

^†† R _free is the same as R _cryst but for 5.1% of the total reflections chosen at random and omitted from refinement

^‡‡This value represents the total B and includes both TLS and residual B components.

^§§Estimated overall coordinate error (Collaborative Computational Project, Number 4, 1994 ▶; Cruickshank, 1999 ▶).