4lzt
From Proteopedia
(New page: 200px<br /><applet load="4lzt" size="450" color="white" frame="true" align="right" spinBox="true" caption="4lzt, resolution 0.95Å" /> '''ATOMIC RESOLUTION RE...) |
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| - | [[Image:4lzt.jpg|left|200px]]<br /><applet load="4lzt" size=" | + | [[Image:4lzt.jpg|left|200px]]<br /><applet load="4lzt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4lzt, resolution 0.95Å" /> | caption="4lzt, resolution 0.95Å" /> | ||
'''ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K'''<br /> | '''ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray diffraction data have been collected at both low (120 K) and room | + | 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 > 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. |
==About this Structure== | ==About this Structure== | ||
| - | 4LZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | + | 4LZT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=NO3:'>NO3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LZT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lamzin, V.]] | [[Category: Lamzin, V.]] | ||
[[Category: Schneider, T.]] | [[Category: Schneider, T.]] | ||
| - | [[Category: Sieker, L | + | [[Category: Sieker, L C.]] |
| - | [[Category: Walsh, M | + | [[Category: Walsh, M A.]] |
| - | [[Category: Wilson, K | + | [[Category: Wilson, K S.]] |
[[Category: NO3]] | [[Category: NO3]] | ||
[[Category: glycosidase]] | [[Category: glycosidase]] | ||
| Line 25: | Line 25: | ||
[[Category: o-glycosyl]] | [[Category: o-glycosyl]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:48 2008'' |
Revision as of 17:13, 21 February 2008
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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 > 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.
About this Structure
4LZT is a Single protein structure of sequence from Gallus gallus with as ligand. Active as Lysozyme, with EC number 3.2.1.17 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 Feb 21 19:13:48 2008
Categories: Gallus gallus | Lysozyme | Single protein | Dauter, Z. | Lamzin, V. | Schneider, T. | Sieker, L C. | Walsh, M A. | Wilson, K S. | NO3 | Glycosidase | Hydrolase | O-glycosyl
