Table 3.
Summary information for the first 27 proteins crystallized and solved by the NYSGRC
| Range of Organisms | |
| S. cerevisiae | 12 |
| Eubacteria | 8 |
| Archaea | 3 |
| Human or mouse | 4 |
| Methods of structure determination | |
| MAD/Se | 18 |
| MAD/MIR other elements | 1 |
| SIRAS | 4 (Pt or Hg) |
| MIR | 1 |
| MR from NYSGRC structure | 2 |
| Part of larger complex | 1 |
| Crystal systems | |
| Monoclinic | 5 |
| Orthorhombic | 11 |
| Tetragonal | 5 |
| Trigonal or hexagonal | 6 |
| Size of the recombinant protein crystallized | 280 residues |
| Resolution limit of the diffraction sample | 2.3 Å |
| Unit cell dimension | 86 Å |
| Longest unit cell dimension | 509 Å |
| Number of residues/asymmetric unit | 700 |
| Number of protomers/asymmetric unit | 2.5 |
(MAD) multiple wavelength anomalous dispersion; (MIR) mammalian-wide interpersed repeat; (NYSGRC) New York State Genomics Research Consortium; (Se) selenium; (SIRAS) single isomorphous replacement anomalous scattering.