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. Author manuscript; available in PMC: 2009 Dec 11.
Published in final edited form as: Proteins. 2006 Jun 1;63(4):1097–1101. doi: 10.1002/prot.20589

TABLE I.

Summary of the YfiH Crystal Data and SAD Data Collection

Unit cell parameters a = 43.874, b = 50.583, c = 55.347 Å
α = 90.32°, β = 96.32°, γ = 90.40°
Space group PI
Molecular weight [243 residues (SeMet)] 26,380 Da
Molecules per asymmetric unit (a.u.) 2
SeMet residues per a.u. 8
SAD data collection
Wavelength (Å)/energy (keV) 0.9793/12.6603
Resolution range (Å) 30–2.01 (2.08–2.01)a
No. of unique reflections 30,856 (2,849)
Completeness (%) 97.4 (89.6)
Rmergeb 0.071 (0.21)
a

In parentheses are statistics for the highest resolution shell.

b

R merge = (|Ihkl − 〈I|)/Ihkl, where the average intensity 〈I〉 is taken over all symmetry equivalent measurements and Ihkl is the measured intensity for any given reflection.