Crystallization and preliminary X-ray diffraction analysis of the ArsC protein from the Escherichia coli arsenical resistance plasmid, R773.
Diffraction data to 3.0 A resolution were collected on crystals of ArsC protein from the conjugative resistance factor R773 which mediates arsenical resistance in the Gram negative bacterium Escherichia coli. The crystal system is tetragonal, a = 116.2 A, c = 145.0 A and the space group is either P4(1)2(1)2 or P4(3)2(1)2. The most probable range for the contents of the asymmetric unit is four to eight ArsC molecules (M(r) = 15,811).
de Mel
V S
VS
Department of Biochemistry, Wayne State University, School of Medicine, Detroit, MI 48201.
Doyle
M A
MA
Gladysheva
T B
TB
Oden
K L
KL
Martin
P D
PD
Rosen
B P
BP
Edwards
B F
BF
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000302:isolation & purification; D001149:Arsenates / Q000494:pharmacology; D053501:Arsenite Transporting ATPases; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000187:drug effects / Q000235:genetics; D016623:Ion Pumps; D009097:Multienzyme Complexes; D011815:R Factors / Q000235:genetics*
D001149:Arsenates; D001426:Bacterial Proteins; D016623:Ion Pumps; D009097:Multienzyme Complexes; D000251:Adenosine Triphosphatases; D053501:Arsenite Transporting ATPases; C025657:arsenic acid