EC Number   |
|---|
   3.1.21.4 | both native enzyme and as selenomethionyl derivative |
| 3.1.21.4 | C-terminal 232-419 amino acids fragment, space group P212121, resolution 2.8 A, one molecule per asymmetric unit |
| 3.1.21.4 | crystal structure of EcoO109I and its complex with DNA |
| 3.1.21.4 | crystal structure of MmeI in complex with its DNA substrate (a 29-mer DNA duplex containing a single MmeI recognition site (TCCGAC)) and an S-adenosylmethionine analog sinefungin. The co-crystals are obtained in the presence of sinefungin and diffracted to 2.6 A resolution with synchrotron radiation. They belong to space group P1 with unit cell dimensions of a = 61.87 A, b = 95.29 A, c = 161.96 A, alpha = 72.84°, beta = 89.15°, and gamma = 71.61°, and contain two MmeI/DNA/sinefungin complexes in the crystallographic asymmetric unit |
| 3.1.21.4 | crystal structures of a specific MspI-DNA complex in a monoclinic space group and an orthorhombic space group, at 1.95 A and 2.7 A resolution, respectively. Native enzyme, Hg(OAc)2 derivatives, CH3HgCl derivatives, Sm(OAc)3 derivative |
| 3.1.21.4 | crystal structures of mutant enzyme Q138F bound to GTTAAC, GTCGAC both with and without Ca2+, as well as the structure of the wild-type HincII bound to GTTAAC |
| 3.1.21.4 | crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage |
| 3.1.21.4 | database information: http://rebase.neb.com |
| 3.1.21.4 | hanging-drop method |
| 3.1.21.4 | mutant R88A |
