Skip to main content
. Author manuscript; available in PMC: 2009 Dec 11.
Published in final edited form as: Biochemistry. 2004 Dec 28;43(51):16193–16202. doi: 10.1021/bi048877o

Table 1.

Summary of Crystal and SAD Data Collection

  unit cell parameters a = 40.50 Å,
   b = 73.88 Å,
   c = 92.25 Å,
   α = β = γ = 90°
  space group P212121
  molecular massa (Da) 33810
  no. of molecules per asymmetric unit 1
  no. of selenomethionine
 residues per asymmetric unit
1
  wavelength (Å) 0.9791
  resolution limit (Å) 1.70
  no. of unique reflections 31255
  overall data completeness (%) 99.4
  overall data redundancy 10.45
  overall Rmerge (%) 6.9
  figure of merit (FOM) 0.2967
  phasing power 1.6309
Refinement Statistics
resolution range (Å) 50.0–1.7 (1.81–1.7)b
no. of reflections (unique) 58916 (9343)b
no. of reflections (observed) 55440 (7699)b
percent reflections observed 94.1 (82.4)b
σ cutoff 0.0
overall R factor (%) 20.0 (30.5)b
Rfree (%) 23.6 (31.6)b
rms deviations from ideal geometry
 bond lengths (Å) 0.006
 angles (deg) 1.3
 dihedrals (deg) 22.6
 impropers (deg) 0.81
no. of protein non-hydrogen atoms 1977
no. of water molecules 292
mean B factor (Å2) 26.5
Ramachandran plot statistics (%)
 residues in most favored regions 98.3
 residues in additional allowed regions 1.7
 residues in disallowed regions 0.0
a

Molecular mass of the polypeptide with 33-residue tag fused to residues 19–280 of GmpC.

b

Values in parentheses are for the highest-resolution shell.

HHS Vulnerability Disclosure