J
Jaru Jancarik
Researcher at University of California, Berkeley
Publications - 28
Citations - 4718
Jaru Jancarik is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Thermotoga maritima & Protein structure. The author has an hindex of 20, co-authored 28 publications receiving 4651 citations. Previous affiliations of Jaru Jancarik include Lawrence Berkeley National Laboratory.
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Journal ArticleDOI
Sparse matrix sampling: a screening method for crystallization of proteins
Jaru Jancarik,Sung-Hou Kim +1 more
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.
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Crystal structure of cyclin-dependent kinase 2.
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.
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Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21.
A. De Vos,Liang Tong,M. V. Milburn,P. M. Matias,Jaru Jancarik,Shigeru Noguchi,Susumu Nishimura,Kazunobu Miura,Eiko Ohtsuka,Sung-Hou Kim +9 more
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.
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Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states.
Weiru Wang,Ho S. Cho,Rosalind Kim,Jaru Jancarik,Hisao Yokota,Henry H. Nguyen,Igor V. Grigoriev,David E. Wemmer,David E. Wemmer,Sung-Hou Kim,Sung-Hou Kim +10 more
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.
Journal ArticleDOI
Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution.
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.