Crystallization and preliminary X-ray analysis of aspartate racemase from Pyrococcus horikoshii OT3.
Aspartate racemase from Pyrococcus horikoshii OT3 (P. AspR) has been crystallized in three crystal forms by the sitting-drop vapour-diffusion method. The crystals belong to the space groups P2(1), P2(1)2(1)2(1) and P3(1)21 (or P3(2)21). The crystals of space group P2(1) diffract X-rays beyond 1.7 A resolution under 90 K liquid-nitrogen cryoconditions with synchrotron radiation and were selected for structure determination. Two heavy-atom derivatives of this crystal form were obtained by the soaking method, which afforded the initial electron-density map.
Liu
L
L
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Iwata
K
K
Kawarabayasi
Y
Y
Kikuchi
H
H
Kita
A
A
Yohda
M
M
Miki
K
K
D000591:Amino Acid Isomerases / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D019711:Pyrococcus / Q000201:enzymology*
D000591:Amino Acid Isomerases; C019749:aspartate racemase