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Table 1 Statistics of crystallographic analysis

From: Crystal structure of HutZ, a heme storage protein from Vibrio cholerae: A structural mismatch observed in the region of high sequence conservation

Data collection

 

Space group

P41

unit cell (Å)

a=b=80.1 c=125.8

Resolution (Å)

50–2.15

Completeness

95.5 (95.9)a

Redundancy

10.0 (7.8)

I/σ(I)

24.5 (7.2)

Rsym (%)b

10.4 (47.4)

Refinement

 

Resolution

50-2.0

Rwork/Rfree (%)c

19.73/23. 51

RMSD

 

Bond lengths (Å)

0.007

Bond angles (°)

1.070

Ramachandran plot (%)d

 

Most favored (%)

92.9

Additionally allowed (%)

6.9

Generously allowed (%)

0.2

Disallowed (%)

0.0

  1. a Values in parentheses are for reflections in the highest resolution shell.
  2. bRsym=∑ hkl ∑ i |I(hkl) i -<I(hkl)>|/∑ hkl ∑I<I(hkl) i >over i observations.
  3. c Value of Rfree for 3.91% of randomly selected reflections excluded from refinement.
  4. d As defined in PROCHECK.
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BMC Structural Biology

ISSN: 1472-6807

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