Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 7): 816-9, 2012 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-22750873
ABSTRACT
An N-terminal fragment of human SHARPIN was recombinantly expressed in Escherichia coli, purified and crystallized. Crystals suitable for X-ray diffraction were obtained by a one-step optimization of seed dilution and protein concentration using a two-dimensional grid screen. The crystals belonged to the primitive tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 61.55, c = 222.81â
Å. Complete data sets were collected from native and selenomethionine-substituted protein crystals at 100â
K to 2.6 and 2.0â
Å resolution, respectively.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ubiquitinas
/
Proteínas de Transporte
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2012
Tipo de documento:
Article