Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution.
about
Disruption of the M949_RS01915 gene changed the bacterial lipopolysaccharide pattern, pathogenicity and gene expression of Riemerella anatipestifer.Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold.HU of Streptococcus pneumoniae Is Essential for the Preservation of DNA Supercoiling.
P2860
Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@ast
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@en
type
label
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@ast
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@en
prefLabel
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@ast
Crystal structure of histone-l ...... s refined to 1.9 Å resolution.
@en
P2093
P2860
P1476
Crystal structure of histone-l ...... ns refined to 1.9 Å resolution
@en
P2093
Indranil Biswas
Nurjahan Mehzabeen
Pierce O'Neil
Scott Lovell
P2860
P304
P356
10.1107/S2053230X1600217X
P577
2016-03-16T00:00:00Z