Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermus thermophilus aspartyl-tRNA synthetase-1.
Growth kinetics and diffraction properties of monoclinic crystals of eubacterial Thermus thermophilus aspartyl-tRNA synthetase-1 (AspRS-1) prepared in the presence of polyethylene glycol and agarose are studied. Their solubility and two-dimensional phase diagram are compared with those of orthorhombic crystals which grow in the presence of sodium formate or ammonium sulfate. The growth mechanism of the novel crystals was monitored by atomic force microscopy. The gel stabilizes the crystal lattice under the cryogenic conditions used for structure determination at high resolution.
Département Mécanismes et Macromolécules de la Synthèse Protéique, UPR 9002, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15 Rue René Descartes, 67084 Strasbourg, France.
D W
DW
Zhu
B
B
Lorber
C
C
Sauter
J D
JD
Ng
P
P
Bénas
C
C
Le Grimellec
R
R
Giegé
D001226:Aspartate-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism*; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004795:Enzyme Stability; D005782:Gels; D007700:Kinetics; D018625:Microscopy, Atomic Force; D009994:Osmolar Concentration; D012685:Sepharose / Q000378:metabolism*; D012995:Solubility; D013696:Temperature; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000201:enzymology*
D005782:Gels; D012685:Sepharose; D001226:Aspartate-tRNA Ligase