New mini- zincin structures provide a minimal scaffold for members of this metallopeptidase superfamily

BMC Bioinformatics

Table 1 Summary of crystal parameters, data collection, and refinement statistics for Acel_2062 from acidothermus cellulolyticus 11b [PDB:3e11]

Data collection	λ ₁MADSe	λ ₂MADSe	λ ₃MADSe
Wavelength (Å)	0.97949	0.91837	0.97897
Resolution range (Å)	29.437-1.800	29.412-1.801	29.399-1.803
No. of observations	49,068	49,153	48,819
No. of unique reflections	19,523	19,533	19,440
Completeness (%)	95.3 (94.6)^a	95.5 (93.5)^a	94.9 (90.2)^a
Mean I/σ(I)	8.50 (1.69)^a	8.31 (1.67)^a	8.08 (1.51)^a
R_sym on I (%)^†	6.3 (48.0)^a	6.4 (45.7)^a	6.8 (55.5)^a
R_meas on I (%)^‡	9.1 (63.8)^a	9.6 (64.7)^a	10.5 (74.3)^a
Highest resolution shell (Å)	1.86-1.80	1.86-1.80	1.86-1.80
Model and refinement statistics
Resolution range (Å)	29.44-1.80
No. of reflections (total)	19,518
No. of reflections (test)	1,004
Completeness (%total)	99.0
Data set used in refinement	λ ₁ MADSe
Cutoff criteria	\|F\| > 0
R _cryst ^¶	0.175
R _free ^§	0.204
Stereochemical parameters
Restraints (RMSD observed)
Bond angle (°)	1.386
Bond length (Å)	0.014
Average isotropic B-value (Å²)	11.273
ESU^†† based on R_free (Å)	0.125
Protein residues/atoms	228/1791
Water/Ions	193

^ahighest resolution shell.
^†R_sym = S|I_i- < I_i > |/S|I_i| where I_i is the scaled intensity of the i^th measurement and < I_i > is the mean intensity for that reflection.
^‡R_meas is the redundancy-independent Rsym. [18, 19].
^¶R_cryst = S| |F_obs|-|F_calc| |/S|F_obs| where F_calc and F_obs are the calculated and observed structure factor amplitudes, respectively.
^§R_free = as for R_cryst, but for 4.9% of total reflections chosen at random and omitted from refinement.
^†This value represents the total B that includes TLS and residual B components.
^‡ESU = Estimated overall coordinate error [20].
Values in parentheses are for the highest resolution shell. Space group: P12₁1. Unit cell parameters: a = 39.03 Å b = 58.82 Å c = 46.93 α = γ = 90° β = 93.51.

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