Skip to main content
. 2012 Dec 25;41(4):2698–2708. doi: 10.1093/nar/gks1322

Table 2.

Crystallographic analysis of HsaDRS2

Data collection statistics
    Beamline SLS/X10A
    Space group (number) P2 (3)
    Unit cell lengths a, b, c (Å) 142.4, 82.6, 146.3
    Unit cell angles α, β, γ (°) 90, 100.4, 90
    Resolution range (Å) 82–3.7
    Highest resolution shell (Å) 3.8–3.7
    Number of observations0 255 882 (9662)
    Number of unique reflections 35 768 (2403)
    Completeness (%) 98.8 (91.2)
    Multiplicity 7.2 (4.0)
    Rmerge/Rmeas (%)a 18.0 (63.9)/19.4 (72.5)
    <I/σ(I)> 9.4 (2.1)
    Crystal mosaicity (°) 0.25
    Asymmetric unit content 2 dimers
    Solvent content (%) 62
Refined atomic structure
    Resolution range (Å) 30–3.7
    R-factor/R-free (%) 22.1/28.0
    Number of protein residues/atoms 4 × 589/18 840
    Rmsd and bonds (Å) and angles (°)° 0.005/1.08
    Ramachandran plotb residues in most favored unfavored regions (%) 89.2/0.2
    PDBid 4AH6

Values in parentheses are for the highest resolution shell.

aRmerge = Σhkl Σi |Ii(hkl) − <I(hkl)>|/Σhkl Σi Ii(hkl) and redundancy-independent; Rmeas = Σhkl (n/n-1)1/2 Σi |Ii(hkl)<I(hkl)>|/Σhkl Σi Ii(hkl).

bAnalysis carried out with Molprobity in Phenix package.