2i17: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2i17.gif|left|200px]]
{{Seed}}
[[Image:2i17.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i17|  PDB=2i17  |  SCENE=  }}  
{{STRUCTURE_2i17|  PDB=2i17  |  SCENE=  }}  


'''Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K'''
===Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K===




==Overview==
<!--  
Two X-ray data sets for a complex of human aldose reductase (h-AR) with the inhibitor IDD 594 and the cofactor NADP(+) were collected from two different parts of the same crystal to a resolution of 0.81 A at 15 and 60 K using cold helium gas as cryogen. The contribution of temperature to the atomic B values was estimated by comparison of the independently refined models. It was found that although being slightly different for different kinds of atoms, the differences (deltaB) in the isotropic equivalents B of atomic displacement parameters (ADPs) were approximately constant (about 1.7 A(2)) for well ordered atoms as the temperature was increased from 15 to 60 K. The mean value of this difference varied according to the number of non-H atoms covalently bound to the parent atom. Atoms having a B value of higher than 8 A(2) at 15 K showed much larger deviations of deltaB from the average value, which might reflect partial occupancy of atomic sites. An analysis of the anisotropy of ADPs for individual atoms revealed an increase in the isotropy of ADPs with the increase of the temperature from 15 to 60 K. In a separate experiment, a 0.93 A resolution data set was collected from a different crystal of the same complex at 100 K using cold nitrogen as a cryogen. The effects of various errors on the atomic B values were estimated by comparison of the refined models and the temperature-dependent component was inferred. It was found that both decreasing the data redundancy and increasing the resolution cutoff led to an approximately constant increase in atomic B values for well ordered atoms.
The line below this paragraph, {{ABSTRACT_PUBMED_17139089}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17139089 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17139089}}


==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Nadp]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:57:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:00:45 2008''

Revision as of 16:00, 28 July 2008

File:2i17.png

Template:STRUCTURE 2i17

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K

Template:ABSTRACT PUBMED 17139089

About this Structure

2I17 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat., Petrova T, Ginell S, Mitschler A, Hazemann I, Schneider T, Cousido A, Lunin VY, Joachimiak A, Podjarny A, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1535-44. Epub 2006, Nov 23. PMID:17139089

Page seeded by OCA on Mon Jul 28 19:00:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2i17&oldid=711179"