Crystallization of an alpha-amylase, AmyA, from the thermophilic halophile Halothermothrix orenii.
This report is the first crystallographic study of an amylase from an organism that is both thermophilic and halophilic. alpha-Amylase from the thermophilic halophile Halothermothrix orenii (AmyA) is a 515-residue protein. It is stable and significantly active at 338 K in starch solution containing NaCl [up to 25%(w/v)]. Purified recombinant AmyA protein crystallizes in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 55.126, b = 61.658, c = 147.625 A, using the hanging-drop vapour-diffusion method. The crystal diffracts X-rays to a resolution limit of 1.89 A.
Li
Nan
N
Laboratory of X-ray Crystallography, Institute of Molecular and Cell Biology, 30 Medical Drive, National University of Singapore, Singapore 117609, Singapore.
Patel
Bharat K C
BK
Mijts
Benjamin N
BN
Swaminathan
Kunchithapadam
K
D001426:Bacterial Proteins; D003013:Clostridium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D000516:alpha-Amylases / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000516:alpha-Amylases