Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusion.
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 orientation of plate-like crystals grown in agarose gel by counter-diffusion. Thus, complete diffraction data were collected at 2.7 A 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 A.
Biertümpfel
Christian
C
European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Basquin
Jérôme
J
Birkenbihl
Rainer P
RP
Suck
Dietrich
D
Sauter
Claude
C
D000595:Amino Acid Sequence; D019611:Archaeoglobus fulgidus / Q000201:enzymology*; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004058:Diffusion; D004587:Electrophoresis, Agar Gel; D004706:Endodeoxyribonucleases / Q000737:chemistry; D004926:Escherichia coli / Q000378:metabolism; D045565:Holliday Junction Resolvases / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011995:Recombination, Genetic; D017386:Sequence Homology, Amino Acid; D017356:Synchrotrons
D004706:Endodeoxyribonucleases; D045565:Holliday Junction Resolvases