TABLE 1.
Khc-73 construct | Microtubule gliding velocitya | Single molecule motilityb |
Sedimentation coefficient | Stokes radius | Molecular mass |
|||
---|---|---|---|---|---|---|---|---|
Velocityc | Run lengthc | Frequency | Calculatedd | Predictede | ||||
μm/s | μm/s | μm | events/axoneme/min | ×10−13s | Å | kDa | kDa | |
1–387-GFP | 1.45 ± 0.07 | 1.57 ± 0.26 | 0.45 ± 0.09 | 0.09 | 3.0 | 42.5 | 84.2 | 70.8 |
1–432-GFP | 1.51 ± 0.02 | 1.58 ± 0.12 | 1.30 ± 0.49 | 0.15 | 3.0 | 43.3 | 85.7 | 76.1 |
1–547-GFP | 1.62 ± 0.10 | 1.33 ± 0.23 | 0.76 ± 0.11 | 0.13 | 3.0 | 44.0 | 87.1 | 88.8 |
1–623-GFP | 1.58 ± 0.04 | 1.54 ± 0.46 | 1.04 ± 0.11 | 0.28 | 3.0 | 45.5 | 90.1 | 97.8 |
1–387-LZ-GFP | N.D. | 1.56 ± 0.15 | 1.51 ± 0.06 | 6.77 | 5.1 | 43.3 | 144.8 | 75.0 |
a Mean ± S.D. shown for >50 measurements.
b Each data set comes from multiple experiments using protein from a single preparation.
c Mean ± S.D. shown for >40 measurements.
d Molecular mass based on the calculation described under “Experimental Procedures.”
e Molecular mass based on the sum of amino acids in the Khc-73 construct, linker, GFP, and His6 affinity tag.