TY - JOUR
T1 - Crystallization and preliminary X-ray data for the A-isozyme of O-acetylserine sulfhydrylase from Salmonella typhimurium
AU - Rao, G. S Jagannatha
AU - Mottonen, James
AU - Goldsmith, Elizabeth J.
AU - Cook, Paul F.
PY - 1993/8/1
Y1 - 1993/8/1
N2 - The A-isozyme of O-acetylserine sulfhydrylase, a pyridoxal phosphate-dependent enzyme isolated from Salmonella typhimurium catalyzes the synthesis of L-cysteine from O-acetyl-L-serine and sulfide. The pyridoxal form of the enzyme has been crystallized in two different forms. One form is in the orthorhombic space group P212121 with cell constants a = 144.4 Å, b = 96.9 Å and c = 54.3 Å and contains two monomers each of molecular weight 34,000 per asymmetric unit. The second form is in a hexagonal space group with unit cell dimensions a = b = 115 Å, and c = 348 Å and contains two 68,000 dimers per asymmetric unit. Complete native enzyme data sets have been collected for both crystal forms using an R-Axis II detector. A search for suitable heavy-atom derivatives is underway. Although both crystal forms diffract X-rays to better than 2.5 Å, the orthorhombic form is more suited to a detailed structural analysis due to the extended lifetime in the X-ray beam and the relative size of the unit cell.
AB - The A-isozyme of O-acetylserine sulfhydrylase, a pyridoxal phosphate-dependent enzyme isolated from Salmonella typhimurium catalyzes the synthesis of L-cysteine from O-acetyl-L-serine and sulfide. The pyridoxal form of the enzyme has been crystallized in two different forms. One form is in the orthorhombic space group P212121 with cell constants a = 144.4 Å, b = 96.9 Å and c = 54.3 Å and contains two monomers each of molecular weight 34,000 per asymmetric unit. The second form is in a hexagonal space group with unit cell dimensions a = b = 115 Å, and c = 348 Å and contains two 68,000 dimers per asymmetric unit. Complete native enzyme data sets have been collected for both crystal forms using an R-Axis II detector. A search for suitable heavy-atom derivatives is underway. Although both crystal forms diffract X-rays to better than 2.5 Å, the orthorhombic form is more suited to a detailed structural analysis due to the extended lifetime in the X-ray beam and the relative size of the unit cell.
KW - Crystallization
KW - O-acetylserine sulfhydrylase
KW - Pyridoxal 5′-phosphate
KW - Salmonella typhimurium
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U2 - 10.1006/jmbi.1993.1358
DO - 10.1006/jmbi.1993.1358
M3 - Article
C2 - 8515470
AN - SCOPUS:0027169519
SN - 0022-2836
VL - 231
SP - 1130
EP - 1132
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 4
ER -