2l5h: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2l5h.png|left|200px]] | [[Image:2l5h.png|left|200px]] | ||
{{STRUCTURE_2l5h| PDB=2l5h | SCENE= }} | {{STRUCTURE_2l5h| PDB=2l5h | SCENE= }} | ||
===Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering=== | ===Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering=== | ||
{{ABSTRACT_PUBMED_21162528}} | {{ABSTRACT_PUBMED_21162528}} | ||
Revision as of 21:45, 25 July 2012
Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering
Template:ABSTRACT PUBMED 21162528
About this Structure
2l5h is a 2 chain structure of Phosphotransferase with sequence from Escherichia coli. Full experimental information is available from OCA.
See Also
Reference
- Takayama Y, Schwieters CD, Grishaev A, Ghirlando R, Clore GM. Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer. J Am Chem Soc. 2010 Dec 16. PMID:21162528 doi:10.1021/ja109866w