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. 2002 Apr;11(4):723–738. doi: 10.1110/ps.4570102

Table 1A.

Summary of crystallographic analysis for GAB protein

Multiple isomorphous replacement
Native (high) 5 mM HgAc 2 mM thimerosal
dMin/λ (Å) 20–2.0/0.9878 20–2.0/0.9878 20–2.0/0.9878
No. of sites 2 2
Rsyma (%) a overall (outer shell) 7.9 (23.9) 4.9 (15.5) 6.3 (19.8)
Coverage (%) overall (outer shell) 96.9 (94.1) 95.8 (94.9) 74.8 (52.1)
I/σ (I) overall (outer shell) 13.0 (4.2) 9.9 (3.8) 9.1 (4.8)
Reflections (total/unique) 442,770/33,222 446,316/32,810 562,379/25,609
Phasing statistics
    MFIDb (%) 16.0 28.1
    Overall phasing powerc (centric/acentric) 1.25/1.18 0.74/1.07
    Mean FOMd (centric/acentric) 0.358/0.371
    Mean FOMd after Solomon 0.63
Refinement
    Resolution range 20–2.0
    No. of reflections >0.0σ 33216
    Total no. atoms/water/Fe(II) 490/320/1
    Re/Rfreef 0.193/0.240
    Rmsdg bond (Å)/angles(°)/B(Å2) 0.009/1.8/1.63

a Rsym = ∑|I-〈I〉|/∑ I, where I = observed intensity, and 〈I〉 = average intensity.

b MFID (mean fractional isomorphous difference) = ∑∥Fph|-|Fp∥/∑|Fp|, where Fp = protein structure factor amplitude and |Fph| = heavy-atom derivative structure factor amplitude.

c Phasing power = root mean square (|Fh|/E, where |Fh| = heavy-atom structure factor amplitude and E = residual lack of closure error.

d Mean FOM = combined figure of merit.

e R based on 95% of the data used in refinement.

f R based on 5% of the data withheld for the cross-validation test.

g Root mean square deviation of bond lengths, angles, and B factors. Rmsd B is combined for side chain/main chain.

Rc = ∑∥Fh(obs)|-|Fh(calc)∥/∑|Fh(obs)| for centric reflections where |Fh(obs)| = observed heavy-atom structure factor amplitude, and |Fh(calc)| = calculated heavy-atom structure factor amplitude.