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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Mol Microbiol. 2010 Nov 2;79(1):119–132. doi: 10.1111/j.1365-2958.2010.07434.x

Table 2.

Crystallographic data.

Dataset Kly18 with Mg2+ Kly18 without Mg2+
Space group / cell constants (a, b, c, in Å; β in ° if ≠90) I4 / 82.79, 85.79, 53.48 C2 / 121.4, 53.1, 86.3, 134.6
Wavelength (Å) 0.9790 0.8726
No. of measurements / unique reflections 153,136 / 21,225 62,645 / 15,411
Resolution range (Å) (outermost shell) a 30.3 – 1.70 (1.79 – 1.70) 45.3 – 2.40 (2.53 – 2.40)
Completeness (%) 99.0 (95.9) 99.3 (95.9)
Rmerge b 0.034 (0.121) 0.088 (0.511)
Rr.i.m. (= Rmeas) b / Rp.i.m. b 0.036 (0.139) / 0.013 (0.065) 0.101 (0.608) / 0.050 (0.322)
Average intensity (<[<I> / σ(<I>)]>) 37.1 (10.8) 14.8 (2.5)
B-Factor (Wilson) (Å2) / Average multiplicity 18.9 / 7.2 (4.4) 38.4 / 4.1 (3.4)
Resolution range used for refinement (Å) ∞ – 1.70 ∞ – 2.40
No. of reflections used (test set) 20,403 (820) 14,703 (708)
Crystallographic Rfactor (free Rfactor) b 0.158 (0.186) 0.189 (0.259)
No. of protein atoms / solvent molecules / 1,328 / 196 / 2,644 / 115 /
  ligands / ions 1 tripeptide (AFT)/ 2 Zn2+, 1 Mg2+, 1 Cl 1 tris, 1 tetrapeptide (AFTS) / 2 Zn2+
Rmsd from target values
  bonds (Å) / angles (°) 0.006 / 1.03 0.013 / 1.32
  bonded B-factors (main chain / side chain) (Å2) 0.46 / 1.23 0.60 / 1.46
Average B-factors for protein / peptide ligand atoms (Å2) 16.6 / 19.6 33.3 / 50.2
Main-chain conformational angle analysis c
  Residues in favored regions / outliers / all residues 160 / 0 / 166 315 / 0 / 332
a

Values in parentheses refer to the outermost resolution shell.

b

For definitions, see Table 1 in (Mallorquí-Fernández et al., 2008).

c

According to MOLPROBITY (Davis et al., 2007).