Data collection and refinement statistics for crystals of the non-nucleotide–bound MiD51, the Xenon derivative used for SAD phasing, and various MiD51–nucleotide complexes
Native MiD51 | Xe derivative | MiD51–GDP | MiD51–ADP | MiD51ΔPEYFP–GDP | MiD51ΔPEYFP–ADP | |
Data collection | ||||||
Wavelength (Å) | 0.9537 | 1.4586 | 0.9537 | 0.9537 | 1.4586 | 1.4586 |
Space group | P1 | P1 | P1 | P1 | P43212 | P43212 |
Cell dimensions | ||||||
a, b, c (Å) | 72.72, 78.73, 79.36 | 73.14, 78.27, 80.42 | 72.34, 79.09, 80.05 | 72.57, 79.26, 79.38 | 57.72, 57.72, 255.40 | 57.53, 57.53, 253.75 |
α, β, γ (°) | 66.26, 84.93, 64.07 | 65.17, 83.79, 62.39 | 65.81, 84.36, 64.08 | 65.44, 84.18, 63.35 | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
Resolution (Å)a | 40.67–2.12 (2.23–2.12) | 45.80–2.60 (2.74–2.60) | 40.00–2.30 (2.42–2.30) | 50.00–2.30 (2.42–2.30) | 50.00–2.55 (2.69–2.55) | 50.00–2.55 (2.69–2.55) |
Rsym or Rmergea | 0.066 (0.500) | 0.059 (0.324) | 0.078 (0.447) | 0.082 (0.489) | 0.086 (0.499) | 0.083 (0.466) |
I/σIa | 11.0 (2.8) | 16.6 (3.6) | 9.4 (2.2) | 10.8 (2.7) | 31.2 (7.9) | 28.7 (7.7) |
Completeness (%)a | 97.3 (97.3) | 84.4 (44.2) | 98.1 (97.6) | 97.8 (97.3) | 100.0 (100.0) | 100.0 (100.0) |
Redundancya | 2.7 (2.8) | 3.5 (3.4) | 2.5 (2.5) | 3.5 (3.5) | 25.9 (27.5) | 22.3 (23.4) |
Refinement | ||||||
Resolution (Å)a | 39.01–2.12 (2.20–2.12) | – | 39.05–2.30 (2.33–2.30) | 39.19–2.30 (2.38–2.30) | 42.82–2.55 (2.71–2.55) | 42.62–2.55 (2.64–2.55) |
No. of reflections | 79,549 | – | 63,108 | 62,135 | 15,007 | 14,827 |
Rwork/Rfree | 0.2228/0.2626 | – | 0.1913/0.2375 | 0.2161/0.2477 | 0.2085/0.2452 | 0.1965/0.2414 |
No. of atoms | ||||||
Protein | 10,892 | – | 10,872 | 10,652 | 2,674 | 2,650 |
Water | 527 | – | 356 | 341 | 114 | 94 |
B factors | ||||||
Protein | 48.81 | – | 48.03 | 45.70 | 56.05 | 52.13 |
Water | 46.81 | – | 44.59 | 37.42 | 52.84 | 53.43 |
RMSDs | ||||||
Bond lengths (Å) | 0.004 | – | 0.005 | 0.006 | 0.003 | 0.005 |
Bond angles (°) | 0.802 | – | 0.90 | 1.028 | 0.761 | 1.005 |
Native MiD51 | Xe derivative | MiD51–GDP | MiD51–ADP | MiD51ΔPEYFP–GDP | MiD51ΔPEYFP–ADP | |
Data collection | ||||||
Wavelength (Å) | 0.9537 | 1.4586 | 0.9537 | 0.9537 | 1.4586 | 1.4586 |
Space group | P1 | P1 | P1 | P1 | P43212 | P43212 |
Cell dimensions | ||||||
a, b, c (Å) | 72.72, 78.73, 79.36 | 73.14, 78.27, 80.42 | 72.34, 79.09, 80.05 | 72.57, 79.26, 79.38 | 57.72, 57.72, 255.40 | 57.53, 57.53, 253.75 |
α, β, γ (°) | 66.26, 84.93, 64.07 | 65.17, 83.79, 62.39 | 65.81, 84.36, 64.08 | 65.44, 84.18, 63.35 | 90.00, 90.00, 90.00 | 90.00, 90.00, 90.00 |
Resolution (Å)a | 40.67–2.12 (2.23–2.12) | 45.80–2.60 (2.74–2.60) | 40.00–2.30 (2.42–2.30) | 50.00–2.30 (2.42–2.30) | 50.00–2.55 (2.69–2.55) | 50.00–2.55 (2.69–2.55) |
Rsym or Rmergea | 0.066 (0.500) | 0.059 (0.324) | 0.078 (0.447) | 0.082 (0.489) | 0.086 (0.499) | 0.083 (0.466) |
I/σIa | 11.0 (2.8) | 16.6 (3.6) | 9.4 (2.2) | 10.8 (2.7) | 31.2 (7.9) | 28.7 (7.7) |
Completeness (%)a | 97.3 (97.3) | 84.4 (44.2) | 98.1 (97.6) | 97.8 (97.3) | 100.0 (100.0) | 100.0 (100.0) |
Redundancya | 2.7 (2.8) | 3.5 (3.4) | 2.5 (2.5) | 3.5 (3.5) | 25.9 (27.5) | 22.3 (23.4) |
Refinement | ||||||
Resolution (Å)a | 39.01–2.12 (2.20–2.12) | – | 39.05–2.30 (2.33–2.30) | 39.19–2.30 (2.38–2.30) | 42.82–2.55 (2.71–2.55) | 42.62–2.55 (2.64–2.55) |
No. of reflections | 79,549 | – | 63,108 | 62,135 | 15,007 | 14,827 |
Rwork/Rfree | 0.2228/0.2626 | – | 0.1913/0.2375 | 0.2161/0.2477 | 0.2085/0.2452 | 0.1965/0.2414 |
No. of atoms | ||||||
Protein | 10,892 | – | 10,872 | 10,652 | 2,674 | 2,650 |
Water | 527 | – | 356 | 341 | 114 | 94 |
B factors | ||||||
Protein | 48.81 | – | 48.03 | 45.70 | 56.05 | 52.13 |
Water | 46.81 | – | 44.59 | 37.42 | 52.84 | 53.43 |
RMSDs | ||||||
Bond lengths (Å) | 0.004 | – | 0.005 | 0.006 | 0.003 | 0.005 |
Bond angles (°) | 0.802 | – | 0.90 | 1.028 | 0.761 | 1.005 |
A single crystal was used for collection of each dataset.
Values in parentheses are for highest-resolution shell.