Muller-Werkmeister HM

References (4)

Title : Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison - Mehrabi_2021_Sci.Adv_7_eabf1380
Author(s) : Mehrabi P , Bucker R , Bourenkov G , Ginn HM , von Stetten D , Muller-Werkmeister HM , Kuo A , Morizumi T , Eger BT , Ou WL , Oghbaey S , Sarracini A , Besaw JE , Pare-Labrosse O , Meier S , Schikora H , Tellkamp F , Marx A , Sherrell DA , Axford D , Owen RL , Ernst OP , Pai EF , Schulz EC , Miller RJD
Ref : Sci Adv , 7 : , 2021
Abstract : For the two proteins myoglobin and fluoroacetate dehalogenase, we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of micron-sized crystals, the same sample delivery device, and the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins, reasonable data statistics can be obtained with approximately 5000 room-temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution.
ESTHER : Mehrabi_2021_Sci.Adv_7_eabf1380
PubMedSearch : Mehrabi_2021_Sci.Adv_7_eabf1380
PubMedID: 33731353
Gene_locus related to this paper: rhopa-q6nam1

Title : Time-resolved crystallography reveals allosteric communication aligned with molecular breathing - Mehrabi_2019_Science_365_1167
Author(s) : Mehrabi P , Schulz EC , Dsouza R , Muller-Werkmeister HM , Tellkamp F , Miller RJD , Pai EF
Ref : Science , 365 :1167 , 2019
Abstract : A comprehensive understanding of protein function demands correlating structure and dynamic changes. Using time-resolved serial synchrotron crystallography, we visualized half-of-the-sites reactivity and correlated molecular-breathing motions in the enzyme fluoroacetate dehalogenase. Eighteen time points from 30 milliseconds to 30 seconds cover four turnover cycles of the irreversible reaction. They reveal sequential substrate binding, covalent-intermediate formation, setup of a hydrolytic water molecule, and product release. Small structural changes of the protein mold and variations in the number and placement of water molecules accompany the various chemical steps of catalysis. Triggered by enzyme-ligand interactions, these repetitive changes in the protein framework's dynamics and entropy constitute crucial components of the catalytic machinery.
ESTHER : Mehrabi_2019_Science_365_1167
PubMedSearch : Mehrabi_2019_Science_365_1167
PubMedID: 31515393
Gene_locus related to this paper: rhopa-q6nam1

Title : The hit-and-return system enables efficient time-resolved serial synchrotron crystallography - Schulz_2018_Nat.Methods_15_901
Author(s) : Schulz EC , Mehrabi P , Muller-Werkmeister HM , Tellkamp F , Jha A , Stuart W , Persch E , De Gasparo R , Diederich F , Pai EF , Miller RJD
Ref : Nat Methods , 15 :901 , 2018
Abstract : We present a 'hit-and-return' (HARE) method for time-resolved serial synchrotron crystallography with time resolution from milliseconds to seconds or longer. Timing delays are set mechanically, using the regular pattern in fixed-target crystallography chips and a translation stage system. Optical pump-probe experiments to capture intermediate structures of fluoroacetate dehalogenase binding to its ligand demonstrated that data can be collected at short (30 ms), medium (752 ms) and long (2,052 ms) intervals.
ESTHER : Schulz_2018_Nat.Methods_15_901
PubMedSearch : Schulz_2018_Nat.Methods_15_901
PubMedID: 30377366
Gene_locus related to this paper: rhopa-q6nam1

Title : Protein crystals IR laser ablated from aqueous solution at high speed retain their diffractive properties: applications in high-speed serial crystallography - Schulz_2017_J.Appl.Cryst_50_1773
Author(s) : Schulz EC , Kaub J , Busse F , Mehrabi P , Muller-Werkmeister HM , Pai EF , Robertson WD , Miller RJD
Ref : Journal of Applied Crystallography , 50 :1773 , 2017
Abstract : In order to utilize the high repetition rates now available at X-ray free-electron laser sources for serial crystallography, methods must be developed to softly deliver large numbers of individual microcrystals at high repetition rates and high speeds. Picosecond infrared laser (PIRL) pulses, operating under desorption by impulsive vibrational excitation (DIVE) conditions, selectively excite the OH vibrational stretch of water to directly propel the excited volume at high speed with minimized heating effects, nucleation formation or cavitation-induced shock waves, leaving the analytes intact and undamaged. The soft nature and laser-based sampling flexibility provided by the technique make the PIRL system an interesting crystal delivery approach for serial crystallography. This paper demonstrates that protein crystals extracted directly from aqueous buffer solution via PIRL-DIVE ablation retain their diffractive properties and can be usefully exploited for structure determination at synchrotron sources. The remaining steps to implement the technology for high-speed serial femtosecond crystallography, such as single-crystal localization, high-speed sampling and synchronization, are described. This proof-of-principle experiment demonstrates the viability of a new laser-based high-speed crystal delivery system without the need for liquid-jet injectors or fixed-target mounting solutions.
ESTHER : Schulz_2017_J.Appl.Cryst_50_1773
PubMedSearch : Schulz_2017_J.Appl.Cryst_50_1773
PubMedID:
Gene_locus related to this paper: rhopa-q6nam1