Diffraction project datasets TM1394_1vq0

  • Method: Molecular Replacement
  • Resolution: 2.2 Å
  • Space group: P 21 21 21
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PDB website for 1VQ0

doi:10.18430/M31VQ0

Project details

Title Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394) from Thermotoga maritima at 2.20 A resolution
Authors Jaroszewski, L., Schwarzenbacher, R., McMullan, D., Abdubek, P., Agarwalla, S., Ambing, E., Axelrod, H., Biorac, T., Canaves, J.M., Chiu, H.J., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hale, J., Hampton, E., Han, G.W., Haugen, J., Hornsby, M., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., Miller, M.D., Moy, K., Nigoghossian, E., Paulsen, J., Quijano, K., Reyes, R., Rife, C., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., Vincent, J., White, A., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Wilson, I.A.
R / Rfree 0.20 / 0.24
Unit cell edges [Å] 76.21 x 101.67 x 113.69
Unit cell angles [°] 90.0, 90.0, 90.0

Dataset 10192_anneal_1_###.img details

Number of frames 101 (1 - 101)
Distance [mm] 350.0
Oscillation width [°] 1.00
Phi [°] 99.0
Wavelength [Å] 0.97912
Equipment BL9-1 at SSRL (Stanford Synchrotron Radiation Laboratory)