Table 1 Data collection and refinement statistics.

From: Crystal Structure of Human Nocturnin Catalytic Domain

 

Human Nocturnin, residues 122–431

Data collection

   Space Group

P41212

Cell dimensions

   a, b, c (Å)

61.4, 61.4, 155.3

   α, β, γ (°)

90.0, 90.0, 90.0

   Resolution (Å)

30.0–2.7 (2.74–2.69)*

   Rpim

0.063 (0.329)

   CC(1/2)

0.954 (0.814)

   I/σI

10.53 (2.05)

   Completeness %

99.9 (99.9)

   Redundancy

5.7 (3.8)

Refinement

   Resolution (Å)

2.7

   No. unique reflections

9,820 (454)

   Rwork/Rfree

0.2522/0.3069

   No. atoms

2,434

   Protein

2,396

   Mg

1

   Water

37

B-factors

   Protein

40.53

   Mg

36.13

   Water

36.27

R.m.s deviations

   Bond lengths (Å)

0.022

   Bond angles (°)

0.7

Ramachandran plot (%)

   Favored

92.7

   Allowed

7.0

   Disallowed

0.3

  1. *Highest-resolution shell is shown in parentheses.
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