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. 2010 May 12;285(31):24078–24088. doi: 10.1074/jbc.M110.106013

TABLE 1.

X-ray data collection, processing, and refinement statistics

Statistics Data set
HaKAT AtKAT2
Data collection and processing
    Collection site ID23, ESRF, France X12, DESY, Germany
    Wavelength (Å) 0.9762 1.0
    Space group P212121 P21
    Unit cell dimensions a = 78.6 Å; b = 100.7 Å; c = 105.3 Å a = 60.8 Å; b = 86.7 Å; c = 72.7 Å; β = 106.7°
    Resolution (Å) 78.6-1.8 (1.9-1.8)a 34.6-1.5 (1.58-1.5)a
    Rmerge (%) 8.6 (51.9)a 7.8 (50.0)a
    Rpimb% 3.8 (26.9)a 3.1 (23.7)a
    Mean (I)/S.D. mean (I) 18.0 (2.6)a 15.2 (2.6)a
    Completeness (%) 99.2 (94.8)a 97.2 (81.2)a
    No. of unique reflections 77,995 112,318
    Multiplicity 8.2 (5.4)a 5.1 (4.3)a
    Wilson B factorc (Å2) 28.44 12.00

Refinement
    No. of non-hydrogen protein atoms 5,875 6,151
    No. of water molecules 709 1,134
    No. of ethylene glycol molecules 0 9
    Rworkd (%) 18.5 (24.4)e 14.9 (20.9)e
    Rfreed (%) 21.6 (28.6)e 17.7 (21.9)e
    S.D.d
        Bond angles (°) 1.020 1.088
        Bond lengths (Å) 0.006 0.006
    Mean Bd (Å2) 33.4 14.3
        Main chain (Å2) 29.8 9.9
        Side chains (Å2) 34.3 14.0
        Solvent (Å2) 44.6 27.5
    Ramachandran plotf
        Most favored (%) 91.8 93.4
        Additionally allowed (%) 7.4 6.0
        Generously allowed (%) 0.5g 0.3g
        Disallowed (%) 0.3h 0.3h

a Numbers in parentheses refer to outer resolution bin.

b Multiplicity-weighted Rmerge (66).

c From Truncate analysis (67).

d From phenix.refine (47).

e Highest resolution bin.

f From ProCheck (68).

g HaKAT Gln135 and AtKAT2 Gln137 adopt strained conformation in active site.

h HaKAT Lys64 and AtKAT2 Lys66 adopt strained conformation in well defined density in tight turn.