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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary crystallographic investigations of avian 5-aminoimidazole-4-carboxamide ribonucleotide transformylase-inosine monophosphate cyclohydrolase expressed in Escherichia coli
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Crystallization and preliminary crystallographic investigations of avian 5-aminoimidazole-4-carboxamide ribonucleotide transformylase-inosine monophosphate cyclohydrolase expressed in Escherichia coli

机译:结晶和初步的晶体鸟类的调查5-aminoimidazole-4-carboxamide核苷酸transformylase-inosine一磷酸cyclohydrolase大肠杆菌中表达

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摘要

ATIC [5-aminoimidazole-4-carboxamide ribonucleotide transformylase (AICAR Tfase)-inosine monophosphate cyclohydrolase (IMPCH)] is a bifunctional enzyme that catalyzes the penultimate and final steps in the de novo purine biosynthesis pathway and thus is an attractive anticancer target. Recombinant avian ATIC has been purified from an Escherichia coli expression system and crystallized in a binary complex with methotrexate (MTX). Crystals were obtained from PEG 4000 or MPEG 5000 buffered at pH 7.0-7.2 and data were collected from a single crystal at 96 K to 2.3 A resolution at the Stanford Synchrotron Radiation Laboratory (SSRL). The crystals are monoclinic and belong to space group P2_1, with unit-cell dimensions a = 65.17, b = 105.93, c = 103.47 A, β=108.27 deg. Assuming two molecules per asymmetric unit, the Matthews coefficient V_m is 2.63 A~3 Da~(-1) and the solvent volume is 52.9%.
机译:ATIC [5-aminoimidazole-4-carboxamide核苷酸transformylase(爱卡Tfase)肌苷一磷酸cyclohydrolase(IMPCH)]是一个双功能酶催化新创的倒数第二个也是最后一个步骤嘌呤生物合成途径,因此是一个有吸引力的抗癌的目标。ATIC已纯化大肠杆菌表达系统和二进制的结晶复杂与甲氨蝶呤(MTX)。获得4000或5000 MPEG缓冲挂钩pH值7.0 - -7.2和数据收集从一个晶体分辨率在2.3在96 K斯坦福同步辐射实验室(SSRL)。单斜晶体,属于空间集团P2_1单胞尺寸= 65.17,b = 105.93, c = 103.47,β= 108.27度。假设每两个分子不对称单位,马修斯系数V_m 2.63 ~ 3哒~ (1)溶剂体积为52.9%。

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