Summary information and primary citation
- PDB-id
-
5t3l;
DSSR-derived features in text and
JSON formats
- Class
- DNA
- Method
- X-ray (1.58 Å)
- Summary
- B-DNA (cgcgaattcgcg)2 soaked with selenourea for 1
min
- Reference
-
Luo Z (2016): "Selenourea:
a convenient phasing vehicle for macromolecular X-ray
crystal structures." Sci Rep,
6, 37123. doi: 10.1038/srep37123.
- Abstract
- Majority of novel X-ray crystal structures of proteins
are currently solved using the anomalous diffraction signal
provided by selenium after incorporation of
selenomethionine instead of natural methionine by genetic
engineering methods. However, selenium can be inserted into
protein crystals in the form of selenourea
(SeC(NH<sub>2</sub>)<sub>2</sub>),
by adding the crystalline powder of selenourea into mother
liquor or cryo-solution with native crystals, in analogy to
the classic procedure of heavy-atom derivatization.
Selenourea is able to bind to reactive groups at the
surface of macromolecules primarily through hydrogen bonds,
where the selenium atom may serve as acceptor and amide
groups as donors. Selenourea has different chemical
properties than heavy-atom reagents and halide ions and
provides a convenient way of phasing crystal structures of
macromolecules.