Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusion

被引：6

作者：

Biertümpfel, C ^{[1
]}

Basquin, J ^{[1
]}

Birkenbihl, RP ^{[1
]}

Suck, D ^{[1
]}

Sauter, C ^{[1
]}

机构：

[1] European Mol Biol Lab, Struct & Computat Biol Programme, D-69117 Heidelberg, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷

关键词：

D O I：

10.1107/S1744309105018269

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Holliday junction-resolving enzymes are ubiquitous proteins that play a key role in DNA repair and reorganization by homologous recombination. The Holliday junction-cutting enzyme (Hjc) from the archaeon Archaeoglobus fulgidus is a member of this group. The first Hjc crystals were obtained by conventional sparse-matrix screening. They exhibited an unusually elongated unit cell and their X-ray characterization required special care to avoid spot overlaps along the c* axis. The use of an arc appended to the goniometric head allowed proper orientatation of plate-like crystals grown in agarose gel by counter-diffusion. Thus, complete diffraction data were collected at 2.7 angstrom resolution using synchrotron radiation. They belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 37.4, c = 271.8 angstrom.

引用

页码：684 / 687

页数：4

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