Crystallization and preliminary X-ray diffraction data of an archaeal asparagine synthetase related to asparaginyl-tRNA synthetase.
The archaebacterial-type asparagine synthetase A from Pyrococcus abyssi (AS-AR), which is related to asparaginyl-tRNA synthetase, was crystallized in two different conditions using the hanging-drop vapour-diffusion method. Crystals belonging to space group C2 with unit-cell parameters a = 103.6, b = 43.3, c = 121.5 A, beta = 112.6 degrees and one dimer per asymmetric unit were obtained in the presence of 2-propanol and PEG 4000 at pH 5.6. Another crystal form was obtained in the presence of dioxan and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 96.8, b = 103.9, c = 98.4 A, beta = 107.5 degrees and two dimers per asymmetric unit. Two different native diffraction data sets were collected to 2.3 and 3.0 A resolution using synchrotron radiation and cryocooling for crystals belonging to space groups C2 and P2(1), respectively.
Charron
Christophe
C
Département 'Mécanismes et Macromolécules de la Synthèse Protéique et Cristallogenèse', UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue René Descartes, F--67084 Strasbourg CEDEX, France.
Roy
Hervé
H
Blaise
Mickaël
M
Giegé
Richard
R
Kern
Daniel
D
D019843:Archaeal Proteins / Q000737:chemistry; D001217:Aspartate-Ammonia Ligase / Q000737:chemistry*; D001226:Aspartate-tRNA Ligase / Q000737:chemistry; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D043903:Pyrococcus abyssi / Q000201:enzymology*; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry
D019843:Archaeal Proteins; D012346:RNA, Transfer, Amino Acyl; D001226:Aspartate-tRNA Ligase; C029194:asparaginyl-tRNA synthetase; D001217:Aspartate-Ammonia Ligase