This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4lzt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4lzt.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4lzt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4lzt| PDB=4lzt | SCENE= }}
{{STRUCTURE_4lzt| PDB=4lzt | SCENE= }}
-
'''ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K'''
+
===ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K===
-
==Overview==
+
<!--
-
X-ray diffraction data have been collected at both low (120 K) and room temperature from triclinic crystals of hen egg-white lysozyme to 0.925 and 0.950 A resolution, respectively, using synchrotron radiation. Data from one crystal were sufficient for the low-temperature study, whereas three crystals were required at room temperature. Refinement was carried out using the programs PROLSQ, ARP and SHELXL to give final conventional R factors of 8.98 and 10.48% for data with F &gt; 4sigma(F) for the low- and room-temperature structures, respectively. The estimated r.m.s. coordinate error is 0.032 A for protein atoms, 0.050 A for all atoms in the low-temperature study, and 0.038 A for protein atoms and 0.049 A for all atoms in the room-temperature case, as estimated from inversion of the blocked least-squares matrix. The low-temperature study revealed that the side chains of 24 amino acids had multiple conformations. A total of 250 waters, six nitrate ions and three acetate ions, two of which were modelled with alternate orientations were located in the electron-density maps. Three sections of the main chain were modelled in alternate conformations. The room-temperature study produced a model with multiple conformations for eight side chains and a total of 139 water molecules, six nitrate but no acetate ions. The occupancies of the water molecules were refined in both structures and this step was shown to be meaningful when assessed by use of the free R factor. A detailed description and comparison of the structures is made with reference to the previously reported structure refined at 2.0 A resolution.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9761848}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9761848 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9761848}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: O-glycosyl]]
[[Category: O-glycosyl]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:26:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:43:45 2008''

Revision as of 10:43, 3 July 2008

Image:4lzt.png

Template:STRUCTURE 4lzt

ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K

Template:ABSTRACT PUBMED 9761848

About this Structure

4LZT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Refinement of triclinic hen egg-white lysozyme at atomic resolution., Walsh MA, Schneider TR, Sieker LC, Dauter Z, Lamzin VS, Wilson KS, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):522-46. PMID:9761848

Page seeded by OCA on Thu Jul 3 13:43:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lzt"
Personal tools