Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis.
about
High-syn conformation of uridine and asymmetry of the hexameric molecule revealed in the high-resolution structures of Shewanella oneidensis MR-1 uridine phosphorylase in the free form and in complex with uridineConcerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme
P2860
Crystallization of uridine phosphorylase from Shewanella oneidensis MR-1 in the laboratory and under microgravity and preliminary X-ray diffraction analysis.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
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2012年论文
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name
Crystallization of uridine pho ...... ry X-ray diffraction analysis.
@en
type
label
Crystallization of uridine pho ...... ry X-ray diffraction analysis.
@en
prefLabel
Crystallization of uridine pho ...... ry X-ray diffraction analysis.
@en
P2093
P2860
P921
P1476
Crystallization of uridine pho ...... ry X-ray diffraction analysis.
@en
P2093
Konstantin M Polyakov
Nadezhda N Mordkovich
Tatyana N Safonova
Valentin A Manuvera
Vladimir O Popov
Vladimir P Veiko
P2860
P304
P356
10.1107/S1744309112041784
P577
2012-10-30T00:00:00Z