Mapping enzyme landscapes by time-resolved crystallography with synchrotron and x-ray free electron laser light

MA Wilson - Annual review of biophysics, 2022 - annualreviews.org
Directly observing enzyme catalysis in real time at the molecular level has been a long-
standing goal of structural enzymology. Time-resolved serial crystallography methods at …

Structure of a protein photocycle intermediate by millisecond time-resolved crystallography

UK Genick, GEO Borgstahl, K Ng, Z Ren, C Pradervand… - Science, 1997 - science.org
The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained
light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of …

[20] Cooperativity in enzyme function: Equilibrium and kinetic aspects

KE Nest - Methods in enzymology, 1995 - Elsevier
Publisher Summary Cooperativity in protein or enzyme systems commonly refers to ligand
binding, with the type of positive cooperativity, that gives rise to the sigmoid curves of oxygen …

Mix and inject: reaction initiation by diffusion for time‐resolved macromolecular crystallography

M Schmidt - Advances in Condensed Matter Physics, 2013 - Wiley Online Library
Time‐resolved macromolecular crystallography unifies structure determination with
chemical kinetics, since the structures of transient states and chemical and kinetic …

Laue crystallography: coming of age

Z Ren, D Bourgeois, JR Helliwell, K Moffat… - Journal of …, 1999 - journals.iucr.org
A renewed interest in the Laue diffraction technique has been brought about by the
development of new, more intense and brilliant synchrotron sources along with their …

Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase

JM Bolduc, DH Dyer, WG Scott, P Singer, RM Sweet… - Science, 1995 - science.org
Site-directed mutagenesis and Laue diffraction data to 2.5 Å resolution were used to solve
the structures of two sequential intermediates formed during the catalytic actions of isocitrate …

Millisecond Laue structures of an enzyme–product complex using photocaged substrate analogs

BL Stoddard, BE Cohen, M Brubaker… - Nature structural …, 1998 - nature.com
The structure of a rate-limited product complex formed during a single initial round of
turnover by isocitrate dehydrogenase has been determined. Photolytic liberation of either …

Ultrafast X-ray crystallography and liquidography

H Ki, KY Oang, J Kim, H Ihee - Annual Review of Physical …, 2017 - annualreviews.org
Time-resolved X-ray diffraction provides direct information on three-dimensional structures
of reacting molecules and thus can be used to elucidate structural dynamics of chemical and …

Light-activated proteins

K Curley, DS Lawrence - Current opinion in chemical biology, 1999 - Elsevier
A wide assortment of caged compounds, which are species whose biological activity can be
unleashed with light, have been synthesized and used to investigate a variety of biological …

[HTML][HTML] Caged cysteine and thiophosphoryl peptides

P Pan, H Bayley - FEBS letters, 1997 - Elsevier
Photoreleasable molecules are important in studies of various biological phenomena,
especially cell signaling. Here we report a generally applicable approach …