2czt: Difference between revisions

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==Overview==

Lipocalin-type prostaglandin D synthase is the key enzyme for the, production of prostaglandin D(2), a potent endogenous somnogen, in the, brain. We cloned, produced, and crystallized the native enzyme and, selenomethionyl Cys(65)Ala mutants of the recombinant mouse protein by the, hanging drop vapor-diffusion method with both malonate and citrate as, precipitants. The native crystals obtained with malonate belong to, orthorhombic space group P2(1)2(1)2(1) with lattice constants a = 46.2, b, = 66.8, and c = 105.3 A. The selenomethionyl crystals obtained with, citrate belong to orthorhombic space group C222(1) with lattice constants, a = 45.5, b = 66.8, and c = 104.5 A. The native crystals diffracted beyond, 2.1 A resolution.

Lipocalin-type prostaglandin D synthase is the key enzyme for the production of prostaglandin D(2), a potent endogenous somnogen, in the brain. We cloned, produced, and crystallized the native enzyme and selenomethionyl Cys(65)Ala mutants of the recombinant mouse protein by the hanging drop vapor-diffusion method with both malonate and citrate as precipitants. The native crystals obtained with malonate belong to orthorhombic space group P2(1)2(1)2(1) with lattice constants a = 46.2, b = 66.8, and c = 105.3 A. The selenomethionyl crystals obtained with citrate belong to orthorhombic space group C222(1) with lattice constants a = 45.5, b = 66.8, and c = 104.5 A. The native crystals diffracted beyond 2.1 A resolution.

==About this Structure==

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==Reference==

Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme., Irikura D, Kumasaka T, Yamamoto M, Ago H, Miyano M, Kubata KB, Sakai H, Hayaishi O, Urade Y, J Biochem ~~(Tokyo)~~. 2003 Jan;133(1):29-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761195 12761195]

Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme., Irikura D, Kumasaka T, Yamamoto M, Ago H, Miyano M, Kubata KB, Sakai H, Hayaishi O, Urade Y, J Biochem. 2003 Jan;133(1):29-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761195 12761195]

[[Category: Mus musculus]]

[[Category: Prostaglandin-D synthase]]

Line 21:

[[Category: Kumasaka, T.]]

[[Category: Miyano, M.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Urade, Y.]]

[[Category: Yamamoto, M.]]

Line 30:

[[Category: structural genomics]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Lipocalin-type prostaglandin D synthase is the key enzyme for the, production of prostaglandin D(2), a potent endogenous somnogen, in the, brain. We cloned, produced, and crystallized the native enzyme and, selenomethionyl Cys(65)Ala mutants of the recombinant mouse protein by the, hanging drop vapor-diffusion method with both malonate and citrate as, precipitants. The native crystals obtained with malonate belong to, orthorhombic space group P2(1)2(1)2(1) with lattice constants a = 46.2, b, = 66.8, and c = 105.3 A. The selenomethionyl crystals obtained with, citrate belong to orthorhombic space group C222(1) with lattice constants, a = 45.5, b = 66.8, and c = 104.5 A. The native crystals diffracted beyond, 2.1 A resolution.
+Lipocalin-type prostaglandin D synthase is the key enzyme for the production of prostaglandin D(2), a potent endogenous somnogen, in the brain. We cloned, produced, and crystallized the native enzyme and selenomethionyl Cys(65)Ala mutants of the recombinant mouse protein by the hanging drop vapor-diffusion method with both malonate and citrate as precipitants. The native crystals obtained with malonate belong to orthorhombic space group P2(1)2(1)2(1) with lattice constants a = 46.2, b = 66.8, and c = 105.3 A. The selenomethionyl crystals obtained with citrate belong to orthorhombic space group C222(1) with lattice constants a = 45.5, b = 66.8, and c = 104.5 A. The native crystals diffracted beyond 2.1 A resolution.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme., Irikura D, Kumasaka T, Yamamoto M, Ago H, Miyano M, Kubata KB, Sakai H, Hayaishi O, Urade Y, J Biochem (Tokyo). 2003 Jan;133(1):29-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761195 12761195]
+Cloning, expression, crystallization, and preliminary X-ray analysis of recombinant mouse lipocalin-type prostaglandin D synthase, a somnogen-producing enzyme., Irikura D, Kumasaka T, Yamamoto M, Ago H, Miyano M, Kubata KB, Sakai H, Hayaishi O, Urade Y, J Biochem. 2003 Jan;133(1):29-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12761195 12761195]
 [[Category: Mus musculus]]
 [[Category: Prostaglandin-D synthase]]
@@ Line 21: / Line 21: @@
 [[Category: Kumasaka, T.]]
 [[Category: Miyano, M.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Urade, Y.]]
 [[Category: Yamamoto, M.]]
@@ Line 30: / Line 30: @@
 [[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:51:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:59 2008''