Table 1 Crystallographic statistics for CTX-M-15/BLIP X-ray structure

From: An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes

 

CTX-M-15/BLIP

Data collection

Space group

I 1 2 1

Cell dimensions

 a, b, c (Å)

47.48, 81.86, 129.12

 α, β, γ (°)

90.00 95.94 90.00

Resolution (Å)

34.51–1.40 (1.42–1.40)

Rmerge

0.075 (0.354)

I/σI

14.6 (5.0)

Completeness (%)

98.37 (97.10)

Redundancy

7.0 (6.9)

Refinement

Resolution (Å)

33.49–1.40 (1.45–1.40)

 No. reflections

94919 (9334)

 Rwork

0.1512 (0.1673)

 Rfree

0.1664 (0.1845)

No. atoms

 Protein

3194

 Ligand/ion

0

 Water

770

B-factors (Å2)

 Average

15.27

 Protein

12.18

 Water

28.08

R.m.s. deviations

 Bond lengths (Å)

0.006

 Bond angles (°)

0.95

  1. Values in parentheses are for the highest-resolution shell.
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