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. Author manuscript; available in PMC: 2010 Sep 1.
Published in final edited form as: Nat Struct Mol Biol. 2010 Feb 21;17(3):373–378. doi: 10.1038/nsmb.1761

Table 1.

Data collection and refinement statistics

SeMet crystala
Data collection
Space group     P21
Cell dimensions
a, b, c (Å) 75.8, 79.8, 75.8
a, b, g (°) 90.0, 97.6, 90.0
Wavelength (Å) 0.97957
Resolution (Å) 30-3.1 (3.26-3.10)b
Rmerge 9.0 (52.2)
I / sI 11.9 (1.8)
Completeness (%) [Anomalous] 95.3 (95.3) [89.7]
Redundancy 4.1 (2.7)
Refinement
Resolution (Å) 3.10
No. reflections 14,648
Rwork / Rfree 23.2/28.7
No. atoms
  Protein 4,056c
B-factors
  Protein 48.5
r.m.s. deviations
  Bond lengths (Å) 0.006
  Bond angles (°) 0.91
a

The working data set was obtained by merging of data from two isomorphous selenomethionine (SeMet)-containing crystals.

b

Values in parentheses are for the shell of highest resolution.

c

Two E–G complexes per asymmetric unit.