Jaru Jancarik

TL;DR: A set of screening conditions for initial experiments in protein crystallization has been developed, tested, and is herein presented as discussed by the authors, which are empirically derived based on known or published crystallization conditions of various proteins in the past, so as to sample as large a range of buffer, pH, additive and precipitant variables as possible, using small amounts of proteins.

TL;DR: The crystal structures of the human CDK2 apoenzyme and its Mg2+ATP complex have been determined to 2.4Å resolution and the structure is bi-lobate, like that of the cyclic AMP-dependent protein kinase, but contains a unique helix—loop segment that interferes with ATP and protein substrate binding.

TL;DR: A resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein consists of a six-stranded beta sheet, four alpha helices, and nine connecting loops that indicate additional regions in the molecule that may possibly participate in other cellular functions.

TL;DR: High-resolution structures of PSP from Methanococcus jannaschii are presented, which define the open state prior to substrate binding, the complex with phosphoserine substrate bound, and thecomplex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction.

TL;DR: This PSP structure appears to be a good model for the closed conformation of P-type ATPase, and may resemble the phosphoserine bound state or the state after autodephosphorylation.