EC Number |
---|
3.1.2.20 | - |
3.1.2.20 | by hanging drop vapor diffusion at 4°C. Two RifR polypeptides in the asymmetric unit (P2(1): a=39.5 A, b=94.6 A, c=63.2 A, beta=90.55°) |
3.1.2.20 | crystal structure of Rv0098 bound to dodecanoic acid is shown |
3.1.2.20 | crystallized using the vapour-diffusion hanging-drop technique at pH 7.0 and 17°C. Crystals are diffracted to 2.0 A resolution |
3.1.2.20 | crystals of Se-Met-substituted protein or of the native protein obtained by hanging-drop vapor diffusion, to 1.9 A resolution. Usage of additives (ATP, 4-(2-hydroxyethyl)-1-piperazinepropanesulfonic acid, 2-(N-morpholino)ethanesulfonic acid at pH 5.9, 3-(N-morpholino)propanesulfonic acid, HEPES at pH 7.0, sodium diphosphate, glucose-6-phosphate, nondetergent sulfobetaines 201 or 256, sodium CoA, lithium myristoyl-CoA, lithium benzoyl-CoA and lithium acetyl-CoA), yielding new crystal forms. The PA5185 protein crystallizes in four different forms. Crystal growth of PA5185 optimized by applying additives with chemical similarity to a fragment of a putative PA5185 substrate (CoA or its derivative). Application of function-biased additives can be used as a standard optimization protocol for producing improved diffraction, or new crystal forms, which may lead to better understanding of the biological functions of proteins like PA5185 |
3.1.2.20 | enzyme forms homodimers in crystals. DELTA1-34 deletion mutant is crystallized to 1.45 A resolution |
3.1.2.20 | enzyme forms homodimers in crystals. DELTA1-34 deletion mutant is crystallized to 1.6 A resolution |
3.1.2.20 | hanging drop method, protein solution: 10 mg/ml, 5 mM NH4OH, 2 mM DTT, over equal volume of reservoir solution: 1-2 M NaCl, 0.1 M sodium formate, pH 6.0, 2 mM N,N-dimethyl-dodecylamine oxide-LDAO, few days, X-ray structure determination and analysis |
3.1.2.20 | hanging drop vapor diffusion method |
3.1.2.20 | hanging-drop vapor diffusion method |