Skip to main content
. Author manuscript; available in PMC: 2007 Apr 17.
Published in final edited form as: J Mol Biol. 2006 Nov 18;366(2):563–573. doi: 10.1016/j.jmb.2006.11.057

Table 1.

Statistics of structure determination and refinement

Nativea
(λ=0.9793)
SeMetb
(λ=0.97887)
PCMBSc
(λ=1.5418)
UO2OAc2d
(λ=1.5418)
Resolution (Å) 25–1.5 50–2.0 25–2.2 25–2.5
Completeness (%) 99.9 (99.3)e 99.8 (99.4) 99.8 (99.6) 93.2 (93.9)
Rsym (%)f 7.1 (21.7) 5.5 (21.9) 6.9 (47.7) 5.6 (28.7)
Riso (%)g 31.2 19.2
Number of sites 6 3 1
Refined structure
R (%)h    18.3
Rfree (%)h    21.8
RMSD from ideal values
Bonds (Å)    0.022
Angles (°)    1.982
Ramachandran plot (%)
Most favored    92.6
Allowed regions    6.1
Generous    0.9
Disallowed    0.4
Number of atomsi    2337
a

Collected at NSLS.

b

Collected at CHESS.

c

PCMBS: 4-(Chloromercuri)benzene sulfonic acid, sodium salt; collected in-house on an R-AXIS IV system using CuKα radiation.

d

UO2OAc2: Uranyl acetate dihydrate; collected in-house on an R-AXIS IV system using CuKα radiation.

e

Numbers in parentheses correspond to the highest resolution shell (1.54–1.50 Å for Native, 2.07–2.00 Å for SeMet, 2.28–2.20 Å for PCMBS, and 2.59–2.50 Å for UO2OAc2).

f

Rsym = Σ|I – <I>|/Σ(I), where I is the observed intensity and <I> is the average intensity of symmetry related reflections, respectively.

g

Riso = Σ|FPHFP|/ΣFPH, where FPH and FP are the derivative and native structure factors, respectively.

h

R and Rfree = Σ||Fobs|– k|Fcalc||/ Σ|Fobs|, where 5% of the reflections were omitted for the calculation of Rfree.

i

254 protein residues (14-267), 3 acetate and 226 water molecules.