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. Author manuscript; available in PMC: 2012 Apr 16.
Published in final edited form as: J Mol Biol. 2005 May 13;348(4):971–982. doi: 10.1016/j.jmb.2005.02.057

Table 1.

X-ray data collection statistics (values in parentheses refer to the highest resolution shell)

Protein M. tuberculosis K. pneumoniae
FAD
K. pneumoniae
FADH
Data collection ESRF ID14-2 Inhouse FADH-
Wavelength (Å) 0.933 1.54178 1.54178
Spacegroup P21212 P3221 P3221
Resolution (Å) 24.5-2.25
(2.37-2.25)
39.2-2.00d
(2.12-2.00)d
28.1-2.35
(2.48-2.35)
Cell (Å) a=137.6, b=153.73, c=137.68
α=β=γ=90.0°
a=85.7, b=85.7, c=99.8
α=β=90°, γ=120.0°
a=86.0, b=86.0, c=100.8
α=β=90°, γ=120.0°
Unique reflections 1188969 24352 17405
I/σ 23 (1.1) 25 (4.3) 12 (1.9)
Multiplicity 6.2 (5.3) 17 (9.1) 2.5 (2.5)
Data completeness (%) 89 (85.2) 88 (49)d 100(99.1)
Rmerge (%)a 10.2 (61.4) 4.6 (17.7) 6.4 (47.9)
Refinement
Rfactorb (%) 24.2 (34.9) 19.3 (29.0) 18.7 (27.6)
Rfreec (%) 28.3 (36.1) 24.7 (34.1) 24.3 (34.1)
Rmsd bond distances (Å) 0.014 0.010 0.011
Rmsd angle ° 1.453 1.203 1.230
In Ramachandran
% Core e
% disallowed e

91
0

91
0

89
0
PDB code31 1VOJ 2B17 1USJ
a

Rmerge = Σhkl Σl|Ii − <I>|/ Σhkl Σl <I>, where Ii is an intensity for the ith measurement of a reflection with indices hkl and <I> is the weighted mean of the reflection intensity.

b

Rfactor = Σhkl|Fo(hkl)| − |Fc(hkl)||/ Σhkl| Fo(hkl)|, where Fo and Fc are the observed and calculated structure factors, respectively.

c

Rfree is the crystallographic Rfactor calculated with 5% of the data that were excluded from the structure refinement.

d

Data extend to 2.0Å and were used in refinement. Due to a technical problem with the detector which prevented its distance being changed, these data were collected in the corners and are incomplete. The structure is quoted to 2.2Å as this is the last shell (2.3Å-2.2Å) where completeness is 90% and the overall completeness to 2.2Å is 98%.

e

Core and disallowed areas are defined by PROCHECK32.