1qqw: Difference between revisions

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[[Image:1qqw.~~gif~~|left|200px]]

[[Image:1qqw.png|left|200px]]

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~~==Overview==~~

Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.

==About this Structure==

1QQW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA].

~~==Reference==~~

Structure of human erythrocyte catalase., Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10666617 10666617]

[[Category: Catalase]]

[[Category: Homo sapiens]]

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[[Category: No nadp]]

[[Category: Water]]

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-[[Image:1qqw.gif|left|200px]]
+[[Image:1qqw.png|left|200px]]
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-==Overview==
+{{ABSTRACT_10666617}}
-Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
 ==About this Structure==
 QQW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA].
-==Reference==
-Structure of human erythrocyte catalase., Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10666617 10666617]
 [[Category: Catalase]]
 [[Category: Homo sapiens]]
@@ Line 33: / Line 29: @@
 [[Category: No nadp]]
 [[Category: Water]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:36:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:52:42 2008''