Table 1: Data collection and refinement statistics
2004-07-21809
Data Collection
Ro 48-8071
Lanosterol
Wavelength (Å)
0.92
0.98
Resolution1 (Å)
20-2.20 (2.26-2.20)
20-2.0 (2.09-2.0)
Unique reflections1
60002 (4884)
79898 (9547)
Completeness (%)1
98.0 (97.5)
99.2 (96.3)
Rmerge (%)1,2
9.9 (37.6)
7.6 (48.9)
<I/>1
7.7 (2.5)
14.4 (3.1)
Unit Cell (Space group C2221)
189.9 Å 202.4 Å 62.6 Å
189.6 Å 201.5 Å 62.1 Å
Refinement
Refmac5
autoBUSTER
Resolution (Å)
20-2.2 (2.26-2.20)
20-2.1 (2.155-2.10)
Rcryst1,3
19.2 (26.2)
14.7 (18.8)
Rfree1,4
22.5 (30.2)
18.8 (24.0)
Average B-factor (Ų)
38.1
33.5
R.m.s. deviations from ideality Bond
0.01 / 1.1
0.01 / 1.6
92.3 / 6.4 / 0.3
93.3 / 5.9 / 0.3
lengths (Å) / angles (°)
Main chain dihedral angles (%) Most
favored / allowed / disallowed 5
1
Values in parentheses refer to the highest resolution bins.
2
Rmerge=I-<I>/I where I is intensity.
3
Rcryst=Fo-<Fc>/Fo where Fo is the observed and Fc is the calculated structure factor amplitude.
4
Rfree was calculated based on 5% of the total data omited during refinement. Rfree was not applied during the
automated model building step.
5
Calculated with PROCHECK31. In both structures the only residues in the disallowed regions of the
ramachandran plot are Glu519 and Lys69
1
31.
Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a
program to check the stereochemical quality of protein structure. J. Appl. Crystallogr. 26, 283291 (1993).
2