Abstract
The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli. The protein was purified by affinity and size-exclusion chromatography and was crystallized using the sitting-drop vapour-diffusion method at 293 K. A complete data set was collected to 2.5 A resolution at 110 K. The crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 A.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adaptor Proteins, Signal Transducing / chemistry*
-
Adaptor Proteins, Signal Transducing / isolation & purification*
-
Adaptor Proteins, Vesicular Transport
-
Amino Acid Sequence
-
Chromatography, Gel
-
Crystallization
-
Crystallography, X-Ray
-
Humans
-
Light
-
Molecular Sequence Data
-
Recombinant Proteins / chemistry
-
Scattering, Radiation
-
Sequence Alignment
-
src Homology Domains*
Substances
-
AHI1 protein, human
-
Adaptor Proteins, Signal Transducing
-
Adaptor Proteins, Vesicular Transport
-
Recombinant Proteins