Preliminary X-ray analysis of a new crystal form of recombinant pig kidney DOPA decarboxylase

被引:5
|
作者
Malashkevich, VN
Burkhard, P
Dominici, P
Moore, PS
Voltattorni, CB
Jansonius, JN
机构
[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
[2] Univ Verona, Fac Sci Matemat Fisiche & Nat, I-37134 Verona, Italy
[3] Univ Verona, Fac Med & Chirurg, Ist Chim Biol, I-37134 Verona, Italy
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1999年 / 55卷
关键词
D O I
10.1107/S0907444998006283
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
DOPA decarboxylase is responsible for the synthesis of the key neurotransmitters dopamine and serotonin via decarboxylation of L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan, respectively. The crystals of recombinant DOPA decarboxylase differ from those previously reported for the enzyme purified from pig kidney. They belong to space group P622 with unit-cell dimensions a = b = 302.6, c = 178.1 Angstrom. Both the self-rotation function and the good diffraction quality of these crystals (2.5 Angstrom on a synchrotron source) suggest that there should be at least three protein dimers in the asymmetric unit. Diffraction data sets have been collected for the native enzyme and a heavy-atom derivative.
引用
收藏
页码:568 / 570
页数:3
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