Table 1 Crystallographic data collection and refinement statistics.

From: Understanding the Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H

 

A3H

Data collection

Space group

P21

Cell dimensions

a, b, c (Å)

46.749, 65.006, 65.540

α, β, γ (°)

90.00, 90.08, 90.00

Resolution (Å)

50–2.49 (2.58–2.49)*

Rsym or Rmerge

8.7 (49.1)

I/σI

19.6 (2.5)

Completeness (%)

98.8 (90.9)

Redundancy

6.2 (4.4)

Molecules per ASU

2

Refinement

Resolution (Å)

50–2.49

No. reflections

13746

Rwork/Rfree

21.12/23.48

No. atoms

3009

 Protein

2976

 Ligand/ion

2

Water

31

B-factors

48.0

 Protein

47.95

 Ligand/ion

45.68

Water

52.72

R.m.s. deviations

 Bond lengths (Å)

0.002

 Bond angles (°)

0.551

  1. Structure was determined from a single crystal. *Highest-resolution shell is shown in parentheses.
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