Table 2.

Crystallization and structure determination of GCaMP variants; x-ray data collection and refinement statistics

GCaMP2-T116V, D381YGCaMP5AGCaMP5GGCaMP5HGCaMP2-LIAGCaMP3-KF
PDB ID3SG23SG33SG43SG53SG63SG7
Oligomeric stateMonomerMonomerMonomerDimerDimerMonomer
Data collection
    Radiation sourceAPS 31-IDAPS 31-IDAPS 31-IDAPS 31-IDCopper anodeALS 8.20.2
    Wavelength (Å)0.97930.97930.97930.97931.54181.0000
    Space groupP41212P41212P41212C2C2P212121
    Unit cell dimensions
        a, b, c (Å)119.6, 119.6, 96.9120.4, 120.4, 98.0120.2, 120.2, 97.4128.6, 46.0, 67.4129.0, 47.5, 68.757.4, 61.5, 124.0
        α, β, γ (°)90, 90, 9090, 90, 9090, 90, 9090, 100.2, 9090, 99.7, 9090, 90, 90
    Resolution (Å)23.8–2.0 (2.11–2.0)20.0–2.1 (2.21–2.1)19.7–2.4 (2.53–2.4)20.0–1.9 (2.0–1.9)28.0–1.7 (1.76–1.7)50.0–1.9 (1.97–1.9)
    Rsym0.088 (0.574)0.132 (0.612)0.138 (0.670)0.088 (0.472)0.070 (0.468)0.068 (0.825)
    I/σI20.8 (4.3)15.3 (4.9)14.7 (3.7)10.9 (3.5)15.9 (1.6)10.2 (2.0)
    Completeness (%)99.9 (100)99.9 (100)99.8 (100)99.6 (100)93.9 (73.9)95.5 (95.6)
    Redundancy13 (11.4)13.9 (13.4)13.7 (9.3)5.5 (5.5)6.5 (2.1)7.2 (7.1)
Refinement
    Resolution (Å)2.002.102.401.901.701.90
    Unique reflections455144035226965291844043832056
    Rwork/Rfree0.173/0.2070.165/0.1990.172/0.2130.180/0.2250.203/0.2490.184/0.230
    No. atoms (B-factors (Å2))3465 (33.0)3470 (33.6)3396 (36.5)3228 (19.8)3358 (19.6)3396 (21.2)
        Protein3182 (32.6)3187 (33.4)3167 (36.5)3089 (18.9)3082 (18.3)3206 (20.1)
        Ligand/ion4 (27.5)4 (31.1)4 (33.5)30 (49.6)4 (30.4)4 (34.7)
        Water279 (36.7)279 (35.9)225 (37.0)109 (34.5)272 (35.2)186 (39.6)
    RMSD values
        Bond lengths (Å)0.0270.0280.0240.0220.0250.024
        Bong angles (°)2.022.091.911.902.021.98
    Ramachandran plot
        Favored/outliers (%)97.7/0.395.9/0.395.6/0.599.2/098.7/097.7/0.3
  • Structures of GCaMP variants have been deposited in the Protein Data Bank (http://www.pdb.org/).