Table 3 Data collection and refinement statistics for the crystal structure of LdtMt2C354S in complex with 1 and LdtMt2 in complex with 3

From: Biochemical and crystallographic studies of l,d-transpeptidase 2 from Mycobacterium tuberculosis with its natural monomer substrate

 

LdtMt2C354S – 1 (PDB: 8PXY)

LdtMt2 – 3 (PDB: 8PXZ)

Data collection

  

 Space group

P 21 21 2

P 21 21 2

 Cell dimensions

  

  a, b, c (Å)

76.61, 94.62, 58.79

77.12, 98.83, 59.23

  α, β, γ (°)

90.00, 90.00, 90.00

90.00, 90.00, 90.00

 Resolution (Å)

58.79–2.15 (2.23–2.15)

42.18–1.98 (2.05–1.98)

 Rmerge

0.138 (0.987)

0.135 (1.997)

 I/σI

10.8 (1.1)

12.3 (1.4)

 Completeness (%)

100.0 (97.0)

99.6 (94.2)

 Redundancy

13.2 (13.5)

13.2 (11.1)

Refinement

PHENIX

PHENIX

 Resolution (Å)

58.79–2.15 (2.23–2.15)a

42.18–1.98 (2.05–1.98)a

 No. reflections

23,889 (2322)

31,078 (2883)

 Rwork/Rfree

0.2032/0.2451

0.1848/0.2259

 No. atoms

3073

3069

  Protein

2655

2664

  Ligand/ion

81

53

  Water

337

352

 B-factors

39.90

41.17

  Protein

39.40

40.14

  Ligand/ion

52.91

68.86

  Water

40.73

44.86

 R.m.s. deviations

  

  Bond lengths (Å)

0.003

0.010

  Bond angles (°)

0.55

0.86

  1. aA single crystal was used for each structure. Values in parentheses are for the highest-resolution shell.
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