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. Author manuscript; available in PMC: 2012 Oct 4.
Published in final edited form as: Biochemistry. 2011 Sep 6;50(39):8497–8507. doi: 10.1021/bi2012355

Table 2.

Data collection and refinement statistics for BMP complexes MtOMPDC mutants

S127A I96S I96T L123N L123S V155D V155S
Data collection
Space group P21 P21 P21 P21 P21 P21 P21
No. of molecules 2 2 2 2 2 2 2
in asym. unit
Cell dimensions
    a (Å) 59.89 59.93 59.97 59.92 59.85 59.74 59.71
    b (Å) 64.16 64.34 63.84 63.98 63.93 64.33 64.28
    c (Å) 61.57 61.58 61.58 61.75 61.74 61.55 61.33
    β (°) 115.60 115.86 115.54 115.56 115.57 115.53 115.54
Resolution (Å) 1.32 1.53 1.42 1.42 1.31 1.42 1.32
No. of unique 98290 63155 76659 78628 95704 77594 97409
reflections
Rmerge 0.071 0.087 0.063 0.079 0.089 0.058 0.091
Completeness (%) 99.8 99.4 97.7 99.3 95.5 97.9 99.26
Refinement
Resolution (Å) 25.0-1.32 25.0-1.53 25.0-1.42 25.0-1.42 25.0-1.31 25.0-1.42 25-1.32
Rcryst 0.172 0.161 0.164 0.180 0.165 0.174 0.164
Rfree 0.193 0.186 0.185 0.205 0.177 0.202 0.177
No. atoms
    Protein 3422 3388 3364 3388 3414 3404 3386
    Waters 424 358 393 432 468 387 465
Bound ligand BMP BMP BMP BMP BMP BMP BMP
Ligand atoms 44 44 44 44 44 44 44
R.m.s deviations
    Bond lengths (Å) 0.006 0.006 0.006 0.006 0.006 0.006 0.006
    Bond angles (°) 1.05 1.08 1.09 1.10 1.11 1.07 1.11
PDB entry 3SIZ 3NQC 3NQD 3NQE 3NQF 3NQG 3NQM